BIOCHEMISTRY

EXAM PDF
UPDATED
01. Common properties of enzymes and inorganic
catalysts. The specific properties of enzymes.
• Catalyze only thermodynamically possible reactions
• Are not used or changed during the reaction.
• Don’t change the position of equilibrium and
direction of the reaction
• Usually act by forming a transient complex with the
reactant, thus stabilizing the transition state
Specific properties of enzymes:
• 1. Accelerate reactions in much higher degree than
inorganic catalysts
• 2. Specificity of action
• 3. Sensitivity to temperature
• 4. Sensitivity to pH
02. The structure of simple and complex enzymes.

03. Cofactors, a difference between coenzyme and

prosthetic group.
04. Characteristic of thermolability and specificity of
enzyme action.
Characteristic of thermolability:
➢ Each enzyme has maximum activity at a particular
temperature (optimum temperature)
➢ Most enzymes have temperature optimum of 37 to
40 °C
➢ (there are exceptions)
enzyme basic phosphatase t+50 °C;
muscle miokinase – t 100 °C
most enzymes are inactivated at temperatures above
about 55 to 60 °C, enzymes denatured.

specificity of enzyme action.

1.Absolute – one enzyme acts only on one substrate
(example: urease decomposes only urea; arginase splits
only arginine)
2.Relative – one enzyme acts on different substrates which
have the same bond type (example: pepsin splits
different proteins)
3.Stereospecificity – some enzymes can catalyze the
transformation only substrates which are in certain
geometrical configuration, cis- or trans

05. Active and allosteric sites of enzymes.

Active site – specific region in the enzyme to which
substrate molecule is bound.
A substrate enters the active site of an enzyme.
Allosteric site- the place where the regulator binds is called
allosteric site.
It can lead to activation or inhibition of enzymes.
06. Isoenzymes.
Some metabolic processes are regulated by enzymes that
exist in different molecular forms – isoenzymes.
Isoenzymes - multiple forms of an enzyme which differ in
amino acid sequence but catalyze the same reaction.
Isoenzymes can differ in:
• kinetics,

• regulatory properties,

• the form of coenzyme they prefer and

• distribution in cell and tissues.

Isoenzymes are coded by different genes.

Example: lactate dehydrogenase (LDG)
Lactate + NAD----→pyruvate + NADH + H+
Lactate dehydrogenase – tetramer (four subunits)
composed of two types of polypeptide chains, M
and H.
• Isozymes of lactate dehydrogenase exist in different
proportions in different tissues.
Isoenzymes are important for diagnosis of different
diseases
There are 5 Isozymes of LDG:
 LDG1, LDG2 – heart, brain, kidney, pancreas
 LDG3 –lungs, spleen
 LDG4, LDG5 - liver, muscle
07. The effect of pH on enzyme activity.
Each enzyme has maximum activity at a particular pH
(optimum pH) above or below this pH the activity
declines.
For most enzymes the optimum pH is ~7 (there are
exceptions):
optimal pH for pepsin – 1,5-2,5, for trypsin – 8-9
08. Competitive and non-competitive inhibition of
enzymes.
Competitive inhibition:
•Inhibitor has a structure similar to the substrate thus can
bind to the same active site
•The enzyme cannot differentiate between the two
compounds
•When inhibitor binds, prevents the substrate from
binding
•Inhibitor can be released by increasing substrate
concentration
Non competitive inhibition:
• Binds to an enzyme site different from the active site
• Inhibitor and substrate can bind enzyme at the same
time
•Cannot be overcome by increasing the substrate
concentration.
09. The principle of international classification of
enzymes. Nomenclature of enzymes.
Principle of the international classification
➢ All enzymes are classified into six categories
according to the type of reaction they catalyze
➢ Each enzyme has an official international name
ending in –ase
➢ Each enzyme has classification number consisting
of four digits: EC: 2.3.4.2
➢ First digit refers to a class of enzyme, second - to a
subclass, third – to a subsubclass, and fourth means
the ordinal number of enzymes in subsubclass.
 ➢ There are two ways of naming of enzymes:
1. Common names i.e are formed by adding the
suffix –ase to the name of substrate
Example: - tyrosinase catalyzes oxidation of
tyrosine; - cellulase catalyzes the hydrolysis of
cellulose Common names don’t describe the
chemistry of the reaction.
2. Trivial names i.e. they don’t give information
about the substrate, product or chemistry of
the reaction
Example: pepsin, catalase, trypsin.
010. Classes of enzymes, main functions of every class.
There are six classes of enzymes:
a. Oxidoreductases- catalyze oxidation-reduction
reactions.
Examples: oxidases, peroxidases, dehydrogenases.
b. Transferases- Catalyze group transfer reactions.
Examples- alanine transaminase

c. Hydrolases- Catalyze hydrolysis reactions where

water is the acceptor of the transferred group.
Examples: esterases, peptidaes, glycosidases.
d. Lysases- Catalyze lysis of a substrate, generating a
double bond in a nonhydrolytic, nonoxidative
elimination.

e. Isomerases- Catalyze isomerisation reactions.

Example: Alanine racemase converts L-alanine to D-
alanine
f. Ligases(synthetases)- catalyze ligation or joining of
two substrates.
Such reactions require chemical energy.

011. Diastase of urine, the principle of determination,

using in diagnostics.
➢ Amylase is an enzyme of class hydrolases. (subclass-
glycosidases).
➢ Activity of amylase can be determined in urine of
healthy body.
➢ Activity of amylase in urine is called diastase.
 ➢ Principle & Usage- the determination of diastase
maybe useful for diagnosis of panceatitis( at the first
days of pancreatitis the diastase may be arised in 10-
100 times).
012. Chemical structure of oxido-reductases. Coenzymes.
Subclasses.
➢ Oxidoreductases are a class of enzymes that
catalyze oxidoreduction reactions.
➢ Oxidoreductases catalyze the transfer of electrons
from one molecule (the oxidant) to another
molecule(the reductant).
➢ Oxidorecuctases can be oxidases or
dehydrogenases.
➢ Oxido-reductases may also contain nicotinamide
adenine dinucleotide (NAD) and nicotinamide
adenine dinucleotide phosphate (NADP) as
coenzymes.
These two coenzymes are reffered to as pyridine
coenzymes or pyridine nucleotides, since
nicotinamide is a derivative of pyridine.

Oxidoreductases consist subclasses:

peroxidases, hydroxylases, oxygenases, and reductases.
 a. Peroxidases are localized in peroxisomes, and
catalyzes the reduction of hydrogen peroxide.
b. Hydroxylases add hydroxyl groups to its
substrates.
c. Oxygenases incorporate oxygen from molecular
oxygen into organic substrates.
d. Reductases catalyze reductions, in most cases
reductases can act like an oxidases.
013. Catalase: structure, properties, biological role.
Catalase – It is a metalloenzyme containing iron ion in its
active center. Catalase – iron-porphyrin enzyme (heme
enzyme), which calalyzes very rapid decomposition of
hydrogen peroxide to water and oxygen.
Found in microbodies of animal cells also called
peroxisomes. It is in the large amounts in erythrocytes
and liver.
Catalase protects cells from hydrogen peroxide (H2O2)
molecules by converting them to oxygen (O2) and water
(H2O).
H2O2 can damage DNA.
Oxygen radicals, such as H2O2, are produced by normal
cellular processes.
Since they are dangerous to the cell, they must be
converted into benign molecules.
Catalase is one of the fastest enzymes known. Оxygen
radicals include hydrogen peroxide, superoxide anion
radicals, singlet oxygen, hydroxyl radicals and nitric
oxide.
Catalases are produced by aerobic organisms ranging from
bacteria to man.
It works best at ph 7.

014. Enzymes specific for heart.

Lactate dehydrogenase 1 and 2
015. Enzymes specific for liver;
LDG 4 and LDG5
016. Enzymes specific for pancreas.
LDG1 LDG2
017. The using of enzymes and isoenzymes in diagnostic
purpose.
Using of enzymes in diagnostic purpose is enzymotherapy.
➢ Pepsin & HCl, pancreatin, oraza, panzinorm-
digestive tract diseases.
➢ Trypsin and chymotrypsin- processing of wounds in
burns, ulcers for proteolysis and deleting of
necrotic tissues.
➢ Trypsin, ribonuclease, DNA-ase
 – splitting and deletion of fibrin from pleural cavity,
- for dilution and deleting of sputum from respiratory
ways in acute and chronic respiratory diseases.
- for thrombophlebitis treatment.
➢ Fibrinolysin, streptokinase- splitting of thrombus.
➢ Hyaluronidase- used for the acceleration of
different medicines penetration in biological tissues
as well as for resorption of scars and hematoma.
➢ Cytochrome C- used in intoxication of CO, H2S and
other substances oppressing tissue respiration.
➢ Glucoso-oxidase- used for lavage of wounds and
burns as antiseptic.
➢ Thrombin- used for preventing and stop bleeding.
018. The using of coenzymes, inhibitors of enzymes in
diagnostic purpose.
COENZYMES
ATP- used in heart diseases, muscle dystrophia.
TPP (thiamin pyrophosphate)- used in heart diseases, and
nervous system pathology.
FMN (flavinmononucleotide) -used for treatment of skin
diseases, keratitis, conjunctivitis.
NAD and NADP- used for improvement of oxidative-
reduction processes in organism.
INHIBITORS
kontrical, trasilol- used in acute pancreatitis for inhibition
of trypsin, chemotrypsin activity.
Diacarb – inhibitor of carbohydrase.
This enzyme regulates the metabolism of Na+ and K+ in
kidney canaliculus and diuresis.
019. Molecular basis of phenylketonuria.
Main cause: phenylalanine hydroxylase is absent.
In the absence of this enzyme, a pathway of phenylalanine
breakdown and tyrosine is not formed.
In childhood excess circulating phenylpyruvate impairs
normal brain development, causing severe mental
retardation.
SYMPTOMS:
➢ Mental retardation
➢ Learning disabilities
➢ Epilepsy
➢ Hyperactivity
➢ Behavioral issues
➢ Skin rash or eczema
➢ Tremors or jerky movement of limbs
020. Molecular basis of alkaptonuria.
Main cause: The absence of homogentisic acid 1,2-
dioxygenase cause urinary excretion of phenyl pyruvic
and homogentisic acids.
It is a rare metabolic disease involving a deficiency in
Homogentisic acid oxidase, resulting in the
accumulation of Homogentisic acid.
Symptoms:
➢ Black coloured urine
➢ Ochronosis
➢ Tendinitis
➢ Kidney and prostate stones
➢ Kyphosis or hunchback
➢ Abnormal pigmentation of connective tissue.
 Diagnosis:
Change in colour of the urine on standing to brown or
dark has been the simple traditional method to
identify alkaptonuria.
The urine gives a positive test with ferric chloride and
silver nitrate.
021. Molecular basis of galactosemia.
Main cause: absence of enzyme galactose-1-phosphate
uridylyltransferase causes the increase of D-galactose in
the blood.
Which ultimately causes accumulation of D-galactose in
blood.
Symptoms:
➢ Brain damage
➢ Cataracts
➢ Jaundice
➢ Enlarged liver
➢ Kidney damage
022. Metabolism – general principles of catabolic and
anabolic processes.
Metabolism - is a collection of chemical reactions that
takes place in the body's cells. Metabolism converts the
fuel in the food that we eat into the energy needed to
power everything we do, from moving to thinking to
growing.
Metabolic pathways can be grouped into two paths –
catabolism and anabolism.
Catabolic reactions - degrade large molecules to create
smaller molecules and energy.
Catabolism is characterized by oxidation reactions and by
exergonic reactions that release of free energy which is
transformed to ATP.
Anabolic reactions - synthesize molecules for cell
maintenance, growth and reproduction.
Anabolism is characterized by reduction reactions and by
utilization of energy accumulated in ATP molecules.
Levels of Metabolism Regulation:
1. Nervous system.
2.Endocrine system.
3.Interaction between organs.
4.Cell (membrane) level.
5.Molecular level
023. The stages of catabolism in the organism.
Stage I. Digestion and Hydrolysis Breakdown of
macromolecules (proteins, carbohydrates and lipids to
respective building blocks (specific stage).
Stage II. Degradation Amino acids, fatty acids and glucose
are oxidized to common metabolite (acetyl CoA)
(specific stage).
Stage III. Oxidation Acetyl CoA is oxidized in citric acid cycle
to CO2 and water. As result reduced cofactor, NADH and
FADH2 , are formed which give up their electrons.
Electrons are transported via the tissue respiration chain
and released energy is coupled directly to ATP synthesis
(common stage).
024. The scheme of specific and common pathways of
proteins, carbohydrates and lipids catabolism.
025. Mechanism of oxidative decarboxylation of
pyruvate.
It is the conversion of pyruvic acid to acetyl-CoA.
Occurs inside the mitochondria.
It is an irreversible process. 5 step reaction.
Enzymes: E1 pyruvate dehydrogenase- TPP[prosthetic
group]
E2 = dihydrolipoyl acetyltransferase -lipoamide
E3 = dihydrolipoyl dehydrogenase - FAD
Coenzymes:
TPP (thiamine pyrophosphate),
lipoamide,
HS-CoA,
FAD+,
NAD+.
The building block of
TPP is vitamin B1 (thiamine);
NAD – vitamin B5 (nicotinamide);
FAD – vitamin B2 (riboflavin),
HS-CoA – vitamin B3 (pantothenic acid),
lipoamide – lipoic acid
Step I is catalyzed by pyruvate dehydrogenase, whose
prosthetic group is the coenzyme thiamin
pyrophosphate. Pyruvate undergoes decarboxylation to
yield CO2 and the -hydroxyethyl derivative of the
thiazole ring of thiamin pyrophosphate.

In step II the acetyl group is transferred to the sulfur atom

of lipoic acid, which constitutes the covalently bound
prosthetic group of the second enzyme of the complex,
dihydrolipoyl acetyl transferase.

In step III, the acetyl group is enzymatically transferred

from the lipoic acid to the coenzyme A; the acetyl-CoA
so formed then leaves the enzyme complex in free form.

In step IV the reduce form of the lipoic acid is oxidized to

its disulfide form by transfer of hydrogen atoms to the
third enzyme of the complex, usually known as
dihydrolipoyl dehydrogenase, whose reducible
prosthetic group is tightly bound flavin adenine
dinucleotide (FAD).
V step. The resulting FADH2 is oxidized by NAD+ with
formation of NADH+H.
➢ Acetyl-CoA serves as fuel for the citric acid cycle in
the next stage of cellular respiration. The addition
of CoA helps activate the acetyl group, preparing it
to undergo the necessary reactions to enter the
citric acid cycle.
026. Role of polyenzymatic complex in process of
oxidative decarboxylation of pyruvate.
Pyruvate dehydrogenase complex is a multienzyme
complex containing 3 enzymes, 5 coenzymes and other
proteins.
It catalyzes oxidative decarboxylation of pyruvate to form
acetyl CoA.
Its 3 enzymes are:
Enzymes: E1 pyruvate dehydrogenase- TPP[prosthetic
group]
E2 = dihydrolipoyl acetyltransferase -lipoamide
E3 = dihydrolipoyl dehydrogenase - FAD
Coenzymes:
TPP (thiamine pyrophosphate),
lipoamide,
HS-CoA,
FAD+,
NAD+.
027. The tricarboxylic acid cycle, sequence of the
reactions.
➢ 11 ATP (3 ATP per NADH, and 2 ATP per FADH2 )
are produced during oxidative phosphorylation.
➢ 1 ATP is directly formed in the citric acid cycle.
➢ 1 acetyl CoA generates approximately 12
molecules of ATP.
028. Biological functions of tricarboxylic acid cycle.
➢ It is an amphibolic pathway. [i.e both catabolic and
anabolic].
➢ The cycle is involved in the aerobic catabolism of
carbohydrates, lipids and amino acids.
➢ Intermediates of the cycle are starting points for
many anabolic reactions.
➢ Yields energy in the form of GTP (ATP).
➢ Yields reducing power in the form of NADH2 and
FADH2 .
 ➢ It is a source of biosynthesis of many precursors.
029. NAD- and FAD- dependent reactions of Krebs cycle.
NAD-dependent:
➢ Isocitrate to α-ketoglutarate.
➢ α-ketoglutarate to succinyl CoA
➢ Malate to Oxaloacetate
FAD-dependant:
➢ Succinate to Fumerate
030. Reaction of substrate-level phosphorylation in Krebs
cycle.
Substrate-level phosphorylation- is the formation of ATP
from ADP and phosphate group donated by certain
substrates.
Reactions of substrate-level phosphorylation takes place in
mitochondria matrix (Krebs cycle) or cytoplasm
(glycolysis).
There are only 3 reactions of substrate-level
phosphorylation in the organism.
➢ The 1-st one takes place in the mitochondria
matrix. During the oxidation of alpha-ketoglutarate
in Krebs cycle the succinyl phosphate is formed.
Then succinyl phosphate donates its phosphate
group to GDP to form GTP. GTP interacts with ADP
and as result ATP is formed.
➢ 2-nd reaction - The formation of ATP in reaction of
1,3-diphosphoglycerate with ADP during glycolysis
is another example of substrate-level
phosphorylation.
 ➢ And the 3-rd reaction of substrate-level
phosphorylation takes place during glycolysis too.
In this reaction phosphoenolpyruvate donates its
phosphate group to ADP. As result ATP and
pyruvate are formed.
031. What is macroergic bond? Examples of high energy
compounds.
A bond in chemical compounds, which acts as an energy
accumulator. Macroergic bond is present in some
phosphorus-containing compounds in living organisms,
adenosine triphosphate (ATP).
Macroergic bonds are formed as a result of complex
biochemical processes and break up when energy is

released.
Examples of High-energy compounds:
➢ Phosphoenol Pyruvate[PEP]
➢ 1,3- diphosphoglycerate
➢ Creatine phosphate
032. Ways of ATP formation in the organism: substrate-
level and oxidative phosphorylation reactions.
There are 2 ways of ATP formation in the organism:
oxidative phosphorylation and substrate-level
phosphorylation. Oxidative phosphorylation is the
 formation of ATP from ADP and phosphate at the
expense of the energy yielded by electron transport to
oxygen.
Substrate-level phosphorylation is the formation of ATP
from ADP and phosphate group donated by certain
substrates.
033. Tissue respiration: location in the cell, sequence of
reaction.
Tissue respiration is the release of energy, usually from
glucose, in the tissues of all animals, green plants, fungi
and bacteria. All these living things require energy for
other processes such as growth, movement, sensitivity,
and reproduction. The most efficient form of respiration
is aerobic respiration: this requires oxygen. When
oxygen is not available, some organisms can respire
anaerobically i.e. without air or oxygen. Yeast can
respire in both ways. Yeast gets more energy from
aerobic respiration, but when it runs out of oxygen it
does not die. It can continue to respire anaerobically,
but it does not get so much energy from the sugar. Yeast
produces ethanol (alcohol) when it respires
anaerobically and ultimately the ethanol will kill the
yeast

034. Molecular complexes of inner mitochondrial

membranes: complex I - NADH-CоQ-reductase. And
complex II - succinate-CоQ-reductase.
complex I - NADH-CоQ-reductase
Transfers electrons from NADH to Co Q (ubiquinone)
Consist of: - enzyme NADH dehydrogenase (FMN -
prosthetic group) - iron-sulphur clusters.
NADH reduces FMN to FMNH2 .
Electrons from FMNH2 pass to a Fe-S clusters.
Fe-S proteins convey electrons to ubiquinone.
QH2 is formed.
The flow of two electrons from NADH to coenzyme Q leads
to the pumping of four hydrogen ions out of the matrix.

complex II - succinate-CоQ-reductase.
Transfers electrons from succinate to Co Q.
Form 1 consist of:
- enzyme succinate dehydrogenase (FAD – prosthetic
group)
- iron-sulfur clusters.
Succinate reduces FAD to FADH2 . Then electrons pass to
Fe-S proteins which reduce Q to QH2.
Complex II does not contribute to proton gradient.
035. Molecular complexes of inner mitochondrial
membranes:
complex III - CоQ- cyt.с1- reductase.
Transfers electrons from ubiquinol to cytochrome C.
Consist of:
cytochrome b,
Fe-S clusters and cytochrome c1 .
Cytochromes – electron transferring proteins containing a
heme prosthetic group (Fe2+  Fe3+).
Oxidation of one QH2 is accompanied by the translocation
of 4 H+ across the inner mitochondrial membrane. Two
H+ are from the matrix, two from QH2.
complex IV - cyt. с – oxidase.
Transfers electrons from cytochrome c to O2 .
Composed of: cytochromes a and a3 .
Catalyzes a four-electron reduction of molecular oxygen
(O2 ) to water (H2O):
O2 + 4e- + 4H+ → 2H2O
Translocates 2H+ into the intermembrane space.
Cytochrome c oxidase consists of 13 subunits and contains
two hemes (two iron atom) and three copper ions,
arranged as two copper centers.
Cytochrome c oxidase pumps four additional protons from
the matrix to the cytoplasmic side of the membrane in
the course of each reaction cycle (mechanism under
study). Totally eight protons are removed from the
matrix in one reaction cycle (4 electrons).
036. Mitchell's chemiosmotic theory.
➢ electron transport and ATP synthesis are coupled
by a proton gradient across the inner mitochondrial
membrane.
➢ Mitchell's chemiosmotic hypothesis was the basis
for understanding the actual process of oxidative
phosphorylation.
Mitchell’s postulates for chemiosmotic theory
1. Intact inner mitochondrial membrane is required.
2. Electron transport through the ETC generates a
proton gradient 3. ATP synthase catalyzes the
 phosphorylation of ADP in a reaction driven by
movement of H+ across the inner membrane into
the matrix.
037. Oxidative phosphorylation, mechanism of H+ -ATP-
ase operation.
➢ Oxidative phosphorylation is the process in which ATP
is formed as a result of the transfer of electrons from
NADH or FADH2 to O2 by a series of electron carriers.
➢ The H+ -ATP-ase found in vacuoles of the eukaryote
cell cytoplasm is similar to the archaeal enzyme, and
is thought to reflect the origin from an archaeal
ancestor.
➢ In most systems, the ATP synthase sits in the
membrane (the "coupling" membrane), and catalyses
the synthesis of ATP from ADP and phosphate driven
by a flux of protons across the membrane down the
proton gradient generated by electron transfer.
➢ The flux goes from the protochemically positive (P)
side (high proton electrochemical potential) to the
protochemically negative (N) side. The reaction
catalyzed by ATP synthase is fully reversible, so ATP
hydrolysis generates a proton gradient by a reversal
of this flux.
➢ In some bacteria, the main function is to operate in
the ATP hydrolysis direction, using ATP generated by
fermentative metabolism to provide a proton
gradient to drive substrate accumulation, and
maintain ionic balance.
ADP + Pi + nH+ P <=> ATP + nH+n
 038. Inhibitors of tissue respiration.
Rotenone and barbiturate drug, amytal block electron
transfer in Complex I.
➢ Rotenone is insecticide that strongly inhibits the
electron transport of complex I.
➢ Rotenone is a natural product obtained from the
roots of several species of plants.
Amytal is a barbiturate drug that blocks electron transport
from NADH to coenzyme Q
2 – Thenoyltrifluoroacetone and carboxin specifically block
electron transport in Complex II.
Antimycin A interferes with electron flow through Complex
III.
➢ Antibiotic.
➢ Induces apoptosis.
➢ Inhibits mitochondrial electron transport
specifically between cytochromes b and c.
Cyanide, azide, and carbon monoxide block electron flow in
Complex IV.
➢ Azide and cyanide bind to the iron when the
iron is in the ferric state.
➢ Carbon monoxide binds to the iron when it is
in the ferrous state.
➢ Cyanide and azide are potent inhibitors at this
site which accounts for there acute toxicity.
➢ Carbon monoxide is toxic due to its affinity for
the heme iron of hemoglobin.
 ➢ Carbon monoxide binds to cytochrome a/a3
but less tightly than cyanide.
➢ It also binds to hemoglobin, displacing oxygen.
➢ Symptoms include headache, nausea,
tachycardia, and tachypnea.
➢ Lips and cheeks turn a cherryred color.
➢ Respiratory depression and coma result in
death if not treated by giving oxygen.
➢ Sources of carbon monoxide include:
• Propane heaters and gas grills
• Vehicle exhaust
• Tobacco smoke
• House fires
• Methylene chloride–based paint strippers
Other inhibitors include antimycin (cytochrome
b/c1), doxorubicin (CoQ), and oligomycin (F0).
039. Uncoupling agents of oxidative phosphorylation.
➢ Uncouplers are lipid-soluble aromatic weak acids
➢ Uncouplers deplete proton gradient by
transporting protons across the membrane
2,4-Dinitrophenol
➢ 2,4-Dinitrophenol permeabilizes the inner
mitochondrial membrane to protons, destroying
the proton gradient and uncouples the electron
transport system from the oxidative
phosphorylation.
➢ In this situation, electrons continue to pass through
the electron transport system and reduce oxygen
to water, but ATP is not synthesized in the process.
 Valinomycin
➢ combines with K ions to form a complex that passes
through the inner mitochondrial membrane.
➢ As a proton is translocated out by electron transfer,
a K ion moves in, and the potential across the
membrane is lost.
➢ This reduces the yield of ATP per mole of protons
flowing through ATP synthase (FoF1). In result -
electron transfer and phosphorrylation become
uncoupled.
➢ Valinomycin is a potent antibiotic which acts as a
potassium (K+) ionophor.
Oligomycin
➢ ATP synthase is inhibited by oligomycin which
prevent the influx of protons through ATP
synthase.
➢ Oligomycin is a natural antibiotic isolated from
Streptomyces diastatochromogenes which inhibits
mitochondrial H+-ATP synthase.
➢ It is primarily found to act as an inhibitor of
mitochondrial respiration.
➢ This binding blocks the proton conductance and
inhibits the synthesis of mitochondrial ATP.
040. Oxygen radicals. Free radicals oxidation.
➢ A free radical is any atom or molecule that contains
one or more unpaired electrons.
➢ The unpaired electrons alter the chemical reactivity
of an atom or molecule, usually making it more
reactive than the corresponding non-radical.
 ➢ Free radicals can originate endogenously from
normal metabolic reactions or exogenously as
components of tobacco smoke and air pollutants
and indirectly through the metabolism of certain
solvents, drugs, and pesticides as well as through
exposure to radiation.
➢ The process of damage by free radicals is called
free radical oxidation.
➢ A free radical is stopped when the electron
difference (gaining or losing an electron) is
corrected.
➢ Molecules that can correct the electron difference
are called - Antioxidants.
➢ Antioxidants are found in dark colored vegetables
and fruit and in dietary supplements.
Oxygen radicals
single electron - superoxide anion (O2 -1)
two electrons – peroxide (O2 -2).
➢ O2 .-, O2 2- and, particularly, their reaction
products are harmful to cell components - reactive
oxygen species or ROS.
041. Classification and representatives of carbohydrates.
 042. Digestion of carbohydrates: localization, types,
role of enzymes.
 ➢ The process of digestion starts in the mouth by the
salivary enzyme –amilase. .
➢ The time for digestion in mouth is limited.
➢ Starch in mouth: hydrolyzed by salivary alfa-amylase
into Maltotriose, Dextrin, Maltose
➢ Starch contain : alfa-1,4-glucosidic linkages and
branched chains alfa-1,6 linkages (branch points,
amylopectin) Alfa-amylase: present in saliva and
pancreatic juice.
➢ Specific for internal alfa-1,4-glucosidic bonds
➢ Salivary -amilase is inhibited in stomach due to the
action of hydrochloric acid.
➢ Another -amilase is produced in pancreas and is
available in the intestine
➢ -amilase hydrolyzes the -1-4-glycosidic bonds
randomly to produce smaller subunits like maltose,
dextrines and unbranched oligosaccharides.
➢ -1-6-glycosidic bonds hydrolyze oligo-1,6- glycosidase
➢ The intestinal juice contains enzymes hydrolyzing
disaccharides into monosaccharides (they are produced
in the intestinal wall) – named disaccharidаses
➢ Sucrase hydrolyses sucrose into glucose and fructose
➢ Lactase hydrolyses lactose into glucose and galactose
➢ Maltase hydrolyses maltose into two glucose molecules

043. The mechanism of monosaccharides absorption.

Only monosaccharides are absorbed.
Absorption occurs mostly in duodenum and upper jejanum of
small intestine.
The rate of absorption: galactose > glucose > fructose
Glucose and galactose from the intestine into endothelial
cells are absorbed by secondary active transport.
Fructose is absorbed from intestine into intestinal cells by
facilitated diffusion.
Absorption of glucose from intestinal cells into bloodstream
is by facilitated diffusion.
Transport of glucose from blood into cells of different organs
is mainly by facilitated diffusion.
The protein facilitating the glucose transport is called glucose
transporter (GluT).
GluT are of 5 types.
➢ GluT1 is seen in erythrocytes and endothelial cells;
➢ GluT2 is located mainly in hepatocytes membranes (it
transport glucose into cells when blood sugar is high)
➢ GluT3 is located in neuronal cells (has higher affinity to
glucose);
➢ GluT4 - in muscles and fat cells.
➢ GluT5 – in intestine and kidneys;
In pancreativ β-cells, GLuT 2 and Glucokinase together
function as the Glucose sensor.
044. Decomposition of glucose in anaerobic conditions
(glycolysis): stages and reactions.
Glycolysis – metabolic pathway in which glucose is
transformed to pyruvate with production of a small
amount of energy in the form of ATP or NADH.
Glycolysis is an anaerobic process (it does not require
oxygen).
Glycolysis pathway is used by anaerobic as well as aerobic
organisms.
In eukaryotic cells, glycolysis takes place in the cytosol.
In glycolysis one molecule of glucose is converted into two
molecules of pyruvate.
Pyruvate can be further metabolized to:
(1) Lactate or ethanol (anaerobic conditions)
(2) Acetyl CoA (aerobic conditions)
The glycolytic pathway consist of 11 enzyme-catalyzed
reactions that begin with a glucose and split it into two
molecules of pyruvate.

045. Energetic balance of glycolysis in anaerobic conditions.

Two molecules of ATP are generated for each molecule of
glucose converted to two molecules of lactate. There is no
net production or consumption of NADH.
046. Energetic balance of glycolysis in aerobic conditions.
Biological role of glycolysis.
A net gain of two ATP per molecule of glucose.
Two molecules of NADH are also produced per molecule of
glucose.
Ongoing aerobic glycolysis requires the oxidation of most of
this NADH by the electron transport chain, producing
approximately three ATP for each NADH molecule entering
the chain
Biological role of glycolysis.
➢ Glycolysis – metabolic pathway in which glucose is
transformed to pyruvate with production of a small
amount of energy in the form of ATP or NADH.
➢ Glycolysis is an anaerobic process (it does not require
oxygen).
➢ Glycolysis pathway is used by anaerobic as well as
aerobic organisms.
➢ In glycolysis one molecule of glucose is converted into
two molecules of pyruvate.
➢ In eukaryotic cells, glycolysis takes place in the cytosol.
047. Alcoholic fermentation. Differences of fermentation
and glycolysis.
The conversion of glucose into ethanol is an example of
alcoholic fermentation.
The net result of alcoholic fermentation is:
Glucose+2Pi + 2ADP + 2H+ → 2 ethanol + 2CO2 + 2ATP +
2H2O
The ethanol formed in alcoholic fermentation provides a key
ingredient for brewing and winemaking.
There is no net NADH formation in the conversion of glucose
into ethanol.
Glycolysis Fermentation
1.Glucose conv. To pyruvic 1. Glucose conv to Ethanol
acid
2. 1 molecule of Glucose→2 2. 1 molecule of glucose→2
molecule of pyruvate. molecule of ethanol.
3. NADH is produced. 3. No NADH is produced.

048. The content of glucose in blood. Source of blood

glucose.
➢ Measured by Glucose oxidase method: [more specific
method]
3.3 to 5.5 mmol/l
➢ Measured by orthotoluidinic acid:
4.4 to 6.6 mmol/l
❖ Source of blood glucose.
➢ Absorption in the intestine.
➢ Splitting of glycogen in liver and muscle.
➢ Gluconeogenesis.
➢ Conv. Of galactose, maltose, fructose into glucose.
049. Causes and consequences of hypo- and
hyperglycemia.
Hypo-glycemia
<72 mg/dl
➢ When blood glucose level is low( i.e below 2mmol/l)
CAUSES:
➢ Starvation
➢ Kidney diseases
➢ Overdose of insulin
➢ Longtime physical activity
➢ Disturbance of digestion and absorption of
carbohydrates

Hyper-glycemia
>200mg/dl
➢ When blood glucose level is higher.
There are physiological and pathological hyperglycemia.
• Physiological hyperglycemia - nutritional and
emotional.
• Pathological hyperglycemia –
pancreatic (diabetes mellitus - deficiency of insulin),
nonpancreatic (increased production of hormones
(except insulin), in some liver diseases, excitation of
central nervous system).
Sometimes, hyperglycemia is not the result of diabetes.
❖ Other medical conditions that can cause
hyperglycemia include:
➢ Pancreatitis (inflammation of the pancreas)
➢ Pancreatic cancer
➢ Hyperthyroidism (overactive thyroid gland)
➢ Cushing's syndrome (elevated blood cortisol level)
➢ Severe stresses on the body, such as heart attack,
stroke, trauma, or severe illnesses, can temporarily
lead to hyperglycemia
➢ Taking certain medications, including prednisone,
estrogens, beta-blockers, glucagon, oral
 contraceptives, phenothiazines, and others, can
elevate blood glucose levels.
050. Diagnostic significance of glucose determination in
blood.
The measurement of glucose concentration in blood is
used for diagnostics of diabetes mellitus, steroid
diabetes, Addison disease, some diseases of liver,
functions of endocrine glands.
051. Stage of aerobic oxidation of glucose.
It is the enzymatic breakdown of glucose (C6H12O6) in the
presence of oxygen (O2) to produce cellular energy
(ATP):
C6H12O6 + 6O2 --→6 CO2 + 6H2O + 38 ATP

1. Glycolysis:
• Glycolysis is the anaerobic catabolic reaction of glucose.
• Glycolysis occurs in almost all cells.
• This pathway takes place with or without the presence of
oxygen.
• Aerobic conditions produce pyruvate and anaerobic
conditions produce lactate as the end products of
glycolysis.
• In the eukaryotic cells, glycolysis occurs in the cytosol.
• Glycolysis a process where a molecule of glucose is
converted into two molecules of pyruvic acid.
 2. Tricarboxylic Acid (Kreb's) Cycle:
The TCA cycle is an aerobic pathway which takes place in
an intracellular organelle called the mitochondria. It
takes pyruvate, the incomplete
• a ten-step process that occurs in the cytoplasm
• converts each molecule of glucose to two molecules of
pyruvic acid (a 3- carbon molecule)
• an anaerobic process - proceeds whether or not O2 is
present ; O2 is not required
• net yield of 2 ATP per glucose molecule
• net yield of 2 NADH per glucose (NADH is nicotine
adenine dinucleotide, a coenzyme that serves as a
carrier for H+ ions liberated as glucose is oxidized.) The
pyruvic acid diffuses into the inner compartment of the
mitochondrion where a transition reaction occurs that
serves to prepare pyruvic acid for entry into the next
stage of respiration
• consists of a series of enzymes on the inner
mitochondrial membrane
• electrons are released from NADH and from FADH2 and
as they are passed along the series of enzymes, they
give up energy which is used to fuel a process called
chemiosmosis by which H+ ions are actively transported
across the inner mitochondrial membrane into the outer
mitochondrial compartment.
The H+ ions then flow back through special pores in the
membrane, a process that is thought to drive the
process of ATP synthesis.
• net yield of 34 ATP per glucose molecule
• 6 H2O are formed when the electrons unite with O2 * at
the end of electron transport chain.

052. Energy balance of complete oxidation of glucose to

СО2 and Н2О.
053. Pentose phosphate pathway of carbohydrates
metabolism.
It supplies NADPH for lipid synthesis and pentose for
nucleic acid synthesis.
Role of PPP:
➢ Synthesis of NADPH (for reductive reactions in
biosynthesis of fatty acids and steroids)
➢ Synthesis of Ribose 5-phosphate (for the
biosynthesis of ribonucleotides (RNA, DNA) and
several cofactors)
➢ Pentose phosphate pathway also provides a means
for the metabolism of “unusual sugars”, 4, 5 and 7
carbons
➢ Pentose phosphate pathway does not function in
the production of high energy compounds like ATP.
❖ Occurrence of PPP:
Liver, Adrenal glands, mammary glands, adipose
tissue, RBCs, Ovary, Testes.
It is not present in Skeletal muscles.
❖ It’s all enzymes occur in the cytosol.
❖ It has two phases:
➢ The oxidative phase that generates NADPH
➢ The nonoxidative phase (transketolase/
transaldolase system) that interconvert
phosphorylated sugars.
The Net reaction of PPP:
Glucose + ATP + 2NADP+ + H2O ribose 5-phosphate + CO2
+ 2NADPH + 2H+ + ADP
054. Biosynthesis of glycogen. Regulation of glycogen
synthesis activity.
It is a polysaccharide, (C6H10O5)n, that is the main form of
carbohydrate storage in animals and occurs primarily in
the liver and muscle tissue.
Also called animal starch.
 Synthesis of glycogen granules begins with a core protein
glycogenin. Glucose addition to a granule begins with
glucose 6-phosphate, which is converted to glucose 1-
phosphate and activated to UDP-glucose for addition to
the glycogen chain by glycogen synthase.
Glycogen synthase is the rate-limiting enzyme of glycogen
synthesis. Glycogen synthase forms the α1,4 glycosidic
bond found in the linear glucose chains of the granule.
Glycogen liver Skeletal muscle
Synthase
Activated by insulin Insulin
Inhibited by Glucagon, Epinephrine
epinephrine
➢ In the well-fed state the 55% of glucose after
absorption is taken by liver and deposited as a
glycogen.
➢ Most glucose residues in glycogen are linked by a-
1,4-glycosidic bonds, branches are created by a-1,6-
glycosidic bonds.
➢ Glycogen serves as a buffer to maintain blood-
glucose level.
➢ Stable blood glucose level is especially important
for brain where it is the only fuel.
➢ The glucose from glycogen is readily mobilized and
is therefore a good source of energy for sudden,
strenuous activity.
 Liver (10 % of weight) and skeletal muscles (2 %) – two
major sites of glycogen storage.
055. Catabolism of glycogen: difference from glycolysis.
Catabolism of glycogen is Glycogenolysis
Glycogenolysis Glycolysis
It is a process of It is breakdown of Glucose
breakdown of glycogen into Pyruvate, ATP and
into glucose. NADH
Occurs in cells of Liver and Occurs in Cytoplasm of cells.
Muscles
Products: Glucose-1- Products: Pyruvate, ATP and
Phosphate and NADH
Glycogen(n-1) residues
Energy production along withEnergy Production.
maintainance of blood
glucose level

056. Hormonal regulation of glycogen metabolism.

Regulatory Hormones: Insulin, Glucagon, Epinephrine

• Insulin is produced by β-cells of the pancreas (high levels

are associated with the fed state)
• Insulin increases rate of glucose transport into muscle,
adipose tissue via GluT4 transporter
• Insulin stimulates glycogen synthesis in the liver via the
second messenger phosphatidylinositol 3,4,5-triphosphate
(PIP3 )
• Secreted by the α cells of the pancreas in response to low
blood glucose (elevated glucagon is associated with the
fasted state)
• Stimulates glycogen degradation to restore blood glucose
to steady-state levels
• Only liver cells are rich in glucagon receptors and therefore
respond to this hormone

• Released from the adrenal glands in response to sudden

energy requirement (“fight or flight”)
• Stimulates the breakdown of glycogen to G1P (which is
converted to G6P)
• Increased G6P levels increase both the rate of glycolysis in
muscle and glucose release to the bloodstream from the
liver and muscles
• Both liver and muscle cells have receptors to epinephrine
057. Genetic disorders of glycogen metabolism.
The Important genetic deficiencies are classed as glycogen
storage diseases since all are characterized by an
accumulation of glycogen.

058. Gluconeogenesis. Biological role of this process.

Gluconeogenesis – synthesis of glucose from
noncarbohydrate precursors
➢ Liver and kidney are major sites of glucose
synthesis
➢ Main precursors: lactate, pyruvate, glycerol
and some amino acids
➢ Under fasting conditions, gluconeogenesis
supplies almost all of the body’s glucose
➢ Gluconeogenesis – universal pathway. It
present in animals, microorganisms, plants
and fungi
 ➢ Plants synthesize glucose from CO2 using the
energy of sun, microorganisms – from acetate
and propionate
All cells are dependent on glucose.
Glucose level in blood plasma must be stable.
Brain is especially sensitive to the decrease of glucose level
(the daily glucose requirement of the brain in a typical
adult human being is about 120 g).
Red blood cells use only glucose as a fuel.
160 g of glucose needed daily by the whole body.
During a longer period of starvation organism must
synthesize glucose from smaller noncarbohydrate
precursor molecules
➢ In glycolysis, glucose is converted into pyruvate; in
gluconeogenesis, pyruvate is converted into
glucose.
➢ However, gluconeogenesis is not a reversal of
glycolysis.
059. Diagnostic significance of the glucose measurement
in urine: types of glucosuria.
The normal amount of glucose in urine is 0 to 0.8 mmol/L
(millimoles per liter). A higher measurement could be a
sign of a health problem that is called Glucosuria.
Diabetes is the most common cause of
elevated glucose levels.
2 main types:
Glucosuria with hyperglyscemia
Glucosuria without hyperglycemia
Renal Glucosuria
060. Diabetes mellitus: types, causes, disorders of
metabolism, symptoms, treatment.
Types: Type 1 due to autoimmune destruction of the
islets of Langerhans of the pancreas.
Type 2 diabetes is strongly associated with obesity and
is a result of insulin resistance and insulin
deficiency.
Gestational diabetes.
Cause: deficiency or insufficiency of insulin
Hormones level in blood: decreased level of insulin
Main symptoms: hyperglycemia; glucosuria; polyuria;
ketonemia; ketonuria; acidosis; hunger and thirst,
degeneration of the walls of blood vessels

061. Biochemical differentiation of diabetes mellitus and

diabetes insipidus.
062. Biochemical differentiation of steroid diabetes, liver
diabetes, kidney diabetes .
Steroid diabetes Liver diabetes Kidney diabetes
Cause: use: Cause: : kidney
hyperproduction disturbances of diseases
of corticosteroids glycogen (disturbances of
synthesis in liver glucose
reabsorbtion)
Hormone level in Hormone level in Hormone level in
Blood: increased Blood: normal Blood: normal
level of
corticosteroids
Main symptoms: Main symptoms: Main symptoms:
hyperglycemia; hyperglycemia; glucosuria;
glucosuria; glucosuria; polyuria,
polyuria. polyuria, pathological
 increased level of biochemical and components in
17-ketosteroids clinical urine
in blood and symptoms of
urine, clinical liver diseases
symptoms of
hypercorticism.

063. The glucose-tolerance test

The glucose tolerance test is a medical test in
which glucose is given and blood samples taken afterward
to determine how quickly it is cleared from the blood.
The test is usually used to test for diabetes, insulin
resistance, impaired beta cell function, and
sometimes reactive hypoglycemia and acromegaly, or rarer
disorders of carbohydrate metabolism.
(extra)Proceedure:
Blood sample is drawn from a patient on an empty stomach
and baseline blood glucose level is measured.
Then the patient is given an oral test dose of 1.0 g of glucose
per kilogram of body weight, and blood glucose level is
measured every 30 min for a few hours.
Glucose tolerance curve is built using the results from the
test.
Plot time on the horizontal axis and glucose level measured
at this time on the vertical axis.
Normal glucose tolerance curve has the following features:
– normal fasting blood glucose level;
– a modest rise in the blood sugar level at about 0.5-1 h, but
not exceeding the renal threshold of about 8 to 10
mmol/L, the concentration at which glucose appears in the
urine in most normal individuals;
– the rise in blood glucose is followed by a rapid decrease to
the normal level within a 2– to 2.5-h period.
Diabetic curve shows: 1) a much higher increase of glucose
concentration in blood, which is initially higher than
normal; 2) a more prolonged period of hyperglycemia; 3)
slower decrease.
Diabetic patients also have increased glucosuria after the
GTT.
064. Biological role and classification of lipids.
LIPIDS
➢ Simple Lipids examples: Acylglycerols, steroids,
waxes.
➢ Complex Lipids are of two subtypes:
a. PHOSPHOLIPIDS: ex: glycerophospholipids,
sphingophospholipids.
b. GLYCOLIPIDS: glycosylglycerols,
glycosphingolipids.

 Energetic role (fuel molecules)

 Components of membranes (structural role)
 Precursors for many hormones (steroids)
 Signal molecules (prostaglandins)
 Protective role (lipids surround important organs)
 Enzyme cofactors (vitamin K)
 Electron carriers (ubiquinone)
065. Digestion of lipids: place and state necessary for
normal digestion of lipids.
Digestion of lipids mainly takes place in duodenum of small
intestine.
➢ State necessary for normal digestion of lipids.
pH = 7,5-8
Availability of enzymes (lipase, phospholipase)
Availability of bile acids (for emulsification of fats).

066. Enzymes taking part in lipids digestion.

067. Structure, primary and secondary bile acids, biological

role.
Primary bile acids- Cholic and Deoxycholic Acid.
➢ Primary bile acids are those synthesized by the liver.
Secondary bile acids- Chenodeoxycholic and Lithocholic Acid.
 ➢ In small intestine at the action of microbodies primary
bile acids convert into secondary.
Bile acids are amphipathic molecules that have hydrophobic
and hydrophilic regions, conjugated bile salts site at the
lipid/ water interface.
Bile acids conjugates with glycin and taurine forms bile salts
called Taurocholate and glycocholate.These are the most
abundant bile salts.
Bile salts are also amphipathic, act as detergents emulsifying
the liquid drops and increasing the surface of the interface.
Bile salts also activates the lipase.
They are water insoluble.
Synthesized from cholesterol.

068. Products of lipids digestion, mechanism of their

absorption.
➢ Products of lipids digestion:
➢ Free Fatty acids
➢ 2-Monoacylglycerols
➢ 1-Monoacylglycerols
➢ Glycerol
➢ Free cholesterol
➢ Lysophosphoglycerols
These together with bile salts form mixed micelles.
Fat soluble Vitamins( A, D, E, K) are also packaged along in
these micelles in small amounts.
Lipid absorption – passive diffusion process in micelles
069. Choleinic complexes. Role of hepato-enteral circulation
of bile acids.

Micelles migrate to the microvilli and lipids diffuse into the

cells.
Bile acids are actively absorbed and transferred to the liver
via portal vein.
Bile salts can circulate through intestine and liver 5-10 times
per day.
This process named – enterohepatic circulation
The main role is :
Some of the biliary acids circulate in the intestine which
helps in absorption of fats and other substances.
070. Resynthesis of lipids in enterocytes.
In the intestinal cells the fatty acids are converted to
fatty acyl CoA molecules – active form of fatty acids (enzyme-
acyl-CoA synthase.
Three of these molecules can combine with glycerol, or two
with monoacylglycerol, to form a triacylglycerols.
These reactions are catalyzed by monoacylglycerol
acyltransferase and diacylglycerol acyltransferase
respectively.
071. Oxidation of glycerol, metabolism, energetic balance.
Glycerol is absorbed by the liver.
➢ Steps: phosphorylation, oxidation and isomerisation.
Glyceraldehyde 3-phosphate is an intermediate in:
➢ glycolytic pathway
➢ gluconeogenic pat
072. Beta-oxidation of fatty acids: mechanism, localization
of this process in cells.
Fatty acids are oxidized in several tissues, including liver,
muscle, and adipose tissue, by the pathway of β-oxidation.
Neither erythrocytes nor brain can use fatty acids and so
continue to rely on glucose during normal periods of
fasting.
STAGES:
a. Activation of fatty acids takes place on the outer
mitochondrial membrane
b. Transport into the mitochondria
c. Degradation to two-carbon fragments (as acetyl CoA) in
the mitochondrial matrix (b-oxidation pathway)
 ➢ Each round generates one molecule each of:
FADH2
NADH
Acetyl CoA
Fatty acyl CoA (2 carbons shorter each round)
➢ Fates of the products of b-oxidation:
- NADH and FADH2 - are used in ETC
- acetyl CoA - enters the citric acid cycle
- acyl CoA – undergoes the next cycle of oxidation
073. Energetic value beta-oxidation of fatty acids, role of
vitamins.
074. Oxidation of fatty acids with odd number of carbon
atoms.
 ➢ This process is called Propionic Acid Pathway.
➢ Odd-chain fatty acids occur in bacteria and
microorganisms
➢ Final cleavage product is propionyl CoA rather than
acetyl CoA
➢ Three enzymes convert propionyl CoA to succinyl CoA
(citric acid cycle intermediate)
➢ The propionic acid pathway includes 2 important
enzymes, both in the mitochondria:
➢ Propionyl-CoA carboxylase requires biotin
➢ Methylmalonyl-CoA mutase requires vitamin B12,
cobalamin.
Propionic Acid Pathway:
Step 1: Propionyl CoA is carboxylated to yield the D isomer of
methylmalonyl CoA.
The hydrolysis of an ATP is required.
Enzyme: propionyl CoA carboxylase
Coenzyme: biotin

Step 2: The D isomer of methylmalonyl CoA is racemized to

the L isomer Enzyme: methylmalonyl-CoA racemase
Step 3: L isomer of methylmalonyl CoA is converted into
succinyl CoA by an intramolecular rearrangement
Enzyme: methylmalonyl CoA mutase
Coenzyme: vitamin B12 (cobalamin)

075. Biosynthesis of palmitic acid, localisation in cell.

It is due to de Novo synthesis.
Occurs in liver, adipose tissue, kidney, brain and lactating
mammary glands.
Acetyl CoA is the source of carbon atoms.
Enzymes are located in cytosomal fraction of cells.
It is called as extramitochondrial or cytoplasmic fatty acid
synthase system.
076. Structure and mechanism action of palmitate synthase.
Elongation of fatty acids.
The common product of fatty acid synthesis is palmitate
(16:0).
Cells contain longer fatty acids and unsaturated fatty acids
they are synthesized in the endoplasmic reticulum.
The reactions of elongation are similar to the ones seen with
fatty acid synthase (new carbons are added in the form of
malonyl CoA).
For the formation of unsaturated fatty acids there are various
desaturases catalizing the formation of double bonds.

077. Biosynthesis of triacylglycerols and phospholipids.

Hormonal regulation.
➢ Glycerol 3-phosphate can be obtained either by the
reduction of dihydroxyacetone phosphate (primarily) or
by the phosphorylation of glycerol (to a lesser extent).
• Prolactin. - stimulates synthesis of lipids in mammary
glands
• Lipotropic hormone -stimulates the mobilization of
lipids from depot.
• Thyroxine and triiodthyronine - activate the lipid
oxidation and mobilization.
• Insulin - enhances the synthesis of lipids;
- promotes the lipid storage activating the carbohyd-
rate decomposition;
• Lipocain - activates the formation of phospholipids in
liver and stimulates the action of lipotropic
alimentary factors; - activates the oxidation of fatty
acids in liver.
• Epinephrine - activates the tissue lipase, mobilization
of lipids and oxidation of fatty acids
• Glucocorticoids - promote the absorption of lipids in
intestine; - activate lipolysis; - activate the conversion
of fatty acids in carbohydrates.
 • Sex hormones - enhance the oxidation of lipids; -
inhibit the synthesis of cholesterol
078. Biological role of cholesterol.
➢ Cholesterol is a constituent of membranes and the
source of steroid hormones.
➢ it modulates membrane fluidity over the range of
physiological temperatures.
➢ a precursor of steroid hormones (progesterone,
testosterone, estradiol, cortisol, etc.)
➢ a precursor of bile acids
➢ a precursor of vitamin D
➢ some research indicates cholesterol may act as an
antioxidant
079. Contents of cholesterol in blood, transport forms of
cholesterol.
Normal blood cholesterol level is 5.9 mmol/l or 3 to 5mmol/l
Cholesterol are transported by primary plasma carriers called
LDL.
080. Stages of biosynthesis of cholesterol, localization of
this process.
For one day in the body formed 500 – 800 mg of cholesterol.
About 80 % of this amount are synthesized in the liver, the
rest - in the cells of the mucousa cells of intestine, skin,
adrenal glands, nervous tissue.
Enzymes required for cholesterol synthesis, are in all cells
except red blood cells.
 Three stages of cholesterol biosynthesis
1. From acetyl CoA formed of isopentenyl pyrophosphate,
that is the key building block of cholesterol. (in cytosol)
2. Condensation of six molecules of isopentenyl
pyrophosphate to form squalene (mitochondria)
3. Squalene cyclizes and the tetracyclic product is converted
into cholesterol(mitochondri)
Acetyl CoA (C2 )--→ Isopentenyl pyrophosphate (C5 ) -
→Squalene (C30) -→Cholesterol (C27)
Regulatory enzyme - 3-hydroxy-3-methylglutaryl CoA
reductase.
[Tetrameric enzyme. ]
NADPH - coenzyme
081. Ketone bodies, place and mechanism of ketogenesis.
➢ Ketone bodies are synthesized in liver mitochondria and
exported to different organs.
➢ Ketone bodies are fuel molecules (can fuel brain and
other cells during long starvation)
➢ Ketone Bodies:
a. β-hydroxybutyrate
b. Acetoacetate
c. Acetone
In liver lacks enzyme decomposition of ketones, it cannot
metabolize the ketone bodies.
Ketogenesis takes place in liver but ketogenolysis takes place
in muscle, renal cortex and brain.

082. Mechanisms using of ketone bodies in tissues with the

purpose of energy obtaining (ketolysis).
➢ First way activation: Acetoacetate is activated by the
transfer of CoA from succinyl CoA in a reaction catalyzed
by a specific CoA transferase.
➢ The second way acetoacetyl - CoA is formed by reaction
with CoA with the participation of ATP and the enzyme
acetoacetyl -CoA synthetase.
➢ Acetoacetyl CoA is cleaved by thiolase to yield two
molecules of acetyl CoA (enter the citric acid cycle).
➢ CoA transferase is present in all tissues except liver
083. Mechanism of ketosis at diabetes mellitus and
starvation.

084. Pathologies of lipids metabolism: obesity, fatty liver

degeneration.
Obesity
Obesity means having too much body fat.
Obesity occurs over time when you eat more calories than
you use.
The balance between calories-in and calories-out differs for
each person. Factors that might affect your weight include
your genetic and emotional factors, stress, smoking and
alcoholism, age, overeating, some medicines, eating high-
fat foods, and not being physically active.
Being obese increases your risk of diabetes, heart disease,
infertility, stroke, arthritis, and some cancers.
Fatty liver degeneration
Disbalance in synthesis and breakdown of fats and the
transport of their from the cells leads to fatty liver
degeneration.
In normal state liver contain only 1% of fats.
Increase mobilization of fat from fatty depots and,
consequently, the delay of fat in the liver can occur
diabetes, fasting, deficiensy of choline and proteins,
protein starvation, infection diseases, malignant tumors
also causes fatty liver degenaration.
Substances that prevent fatty liver degeneration, called
lipotropic factors. Lipotropic factors - choline, methionine ,
serine
085. Pathologies of lipids metabolism: atherosclerosis,
hyperketonemia, ketosis.
atherosclerosis
➢ Cholesterol is often deposited on the inner walls of
blood vessels, together with other lipids, a condition
known as atherosclerosis, which often leads to occlusion
 of blood vessels in the heart and the brain, resulting in
heart attacks and strokes, respectively.
➢ Atherosclerosis can lead to serious problems, including
heat attack, stroke, or even death
Hyperketonemia:
➢ It is the acuumulation of ketone bodies in blood.
➢ Causes: fasting, ketogenic diet, diabetes.
Ketosis:
The overall accumulation of ketone bodies in blood and urine
is known - ketosis. The acids also upset buffers in the blood
to cause acidosis (diabets, starvation, alcoholism, smoking,
fatty food, long exercise).

01. Biological role of proteins in the organism.

➢ Antibodies (or Immunoglobulins) - are specialized
proteins involved in defending the body from antigens.
➢ Contractile Proteins - are responsible for movement.
Examples include actin and myosin. These proteins are
involved in muscle contraction and movement.
➢ Energetic function – catabolism of proteins produce 10-
15% of total energy.
 ➢ Enzymes - are proteins that facilitate biochemical
reactions. They are often referred to as catalysts
because they speed up chemical reactions.
➢ Hormonal Proteins - are messenger proteins which help
to coordinate certain bodily activities. Several hormones
are peptides and proteins.
➢ Structural Proteins - are fibrous and stringy and provide
support. Examples: keratins strengthen protective
coverings such as hair, quills.
Collagens and elastin provide support for connective
tissues such as tendons and ligaments.
➢ Storage Proteins - store amino acids. Storing amino acids
as nutrients and as building blocks of cell membranes
for the growing organism.
➢ Transport Proteins - are carrier proteins which move
molecules from one place to another around the body.
Examples - hemoglobin and cytochromes. Hemoglobin
transports oxygen through the blood via red blood cells.
Cytochromes transports Cu2+.
➢ Membrane Proteins: Proteins and lipids are the major
structural components of cell membrane. The
membrane associated proteins consists of intrinsic
proteins and extrinsic proteins.
02. Nitrogenous balance.
Nitrogen balance - the balance between the amount of
nitrogen taken in (foods or the body) and the amount
given off (lost or excreted)
Nitrogen Balance = Nitrogen intake - Nitrogen loss
Positive, negative and neutral (zero).
➢ Positive nitrogen balance is associated with periods of
growth, hypothyroidism, tissue repair and pregnancy,
during recovering after severe diseases, at the using of
anabolic medicines.
This means that the intake of nitrogen into the body is
greater than the loss of nitrogen from the body, so there is
an increase in the total body pool of protein.
➢ Negative nitrogen balance is associated with burns,
serious tissue injuries, fevers, hyperthyroidism, wasting
diseases, during periods of protein starvation and full
fasting, senile age, destroying of malignant tumor,
poisoning by some toxins.
This means that the amount of nitrogen excreted from the
body is greater than the amount of nitrogen ingested.
➢ Zero nitrogenous balance – the amount of nitrogen
removed from the organism is equal to the amount of
nitrogen entered the organism. It occurs in healthy adult
people.
The amount of proteins ingested each day should be in the
range from 80 to 100 g.
03. Essential and nonessential amino acids.
➢ Essential amino acids are those amino acids which are
not synthesized in organism and therefore must be
supplied in the diet.
➢ There are 10 essential amino acids
 ➢ Unessential amino acids can be synthesized in organism
from another compounds.

04. Digestion of proteins in the stomach.

Three enzymes are in gastric juice:
pepsin,
gastricsin and
rennin.
All these enzymes cleave proteins or peptides.
The main enzyme is - pepsin - splits the peptide bonds
between aromatic amino acids as well as the bonds
between residues of alanine, serin and cysteine.
The optimal pH for pepsin activity – 1,5-2,5.
Thus, hydrochloric acid is necessary for pepsin functioning.
 ➢ Chief cells in the gastric glands produce pepsinogen -
inactive form of pepsin. Pepsinogen is converted to
pepsin in the gastric cavity. For this process the ready
pepsin and hydrochloric acid are necessary
(autocatalysis). The peptide chain is split off the
molecule of pepsinogen and rest part gains the enzyme
activity. This part is called pepsin.
➢ Gastricsin also known as pepsinogen C is an enzyme that
in humans is encoded by the PGC gene.
Optimal pH for gastricsin is 2,0-3,0.
Stimulates parietal cells to secrete HCI.
➢ Rennin also possesses a proteolytic activity and causes a
rapid coagulation of ingested casein (milk protein).
But this enzyme plays important role only in children
because the optimal pH for it is 5-6
05. Digestion of proteins in the small intestine.
Most of the digestion proteins is carried out into the small
intestine by pancreatic zymogens trypsinogen,
chymotrypsinogen, proelastase and procarboxypeptidase.
Bicarbonate changes the pH to about 7.
Trypsinogen is produced by pancreas.
This is not active form of enzyme.
Enzyme enterokinase is secreted by the mucosal cells of the
small intestine. Enterokinase split off part of polipeptade
chain from trypsinogen and as result the active trypsin is
formed.
The optimal pH for trypsin – 7,8.
➢ Trypsin converts chymotrypsinogen into chymotrypsin,
procarboxypeptidase into carboxypeptidase and
proelastase into elastase,
and trypsinogen into more trypsin.
Trypsin cleaves peptide bonds between basic amino acids Lys
and Arg
➢ Chymotrypsin is also produced by pancreas in inactive
form (chymotrypsinogen).
Under the effect of trypsin it undergoes the hydrolysis and
active form chymotrypsin is produced.
Chymotrypsin like trypsin also is endopeptidase.
Chymotrypsin cleaves the bonds between aromatic amino
acids Phe, Tyr and Trp
➢ Dipeptides of different size and structure are finally
decompoused in small intestine by peptidases.
Peptidases splitting the amino acid from the end of free
COOH group are called carboxipeptidases and those, which
split amino acid residue from the end of free NH2 group
are called aminopeptidases.
➢ Dipeptidases are enzymes secreted by enterocytes into
the small intestine. Dipeptidases hydrolyze bound pairs
of amino acids, called dipeptides (glycinserine,
valinthreonine).
Dipeptidases are secreted on to the brush border of the villi
in the small intestine, where they cleave dipeptides into
their two component amino acids prior to absorption.
06. Chemical composition of digestion juices.
Gastric juice contains water, enzymes, hydrochloric acid,
mineral salts and other compounds. About 2,5 l of gastric
juice is secreted per day.
Intestinal juice contains water, enzymes, bile, mineral salts,
some tissue hormones and other compounds.
07. Role of hydrochloric acid in protein digestion.
a. Denaturate proteins (denaturated proteins easier
undergo digestion by pepsin than native proteins).
b. Stimulates the activity of pepsin.
c. Hydrochloric acid has bactericidial properties.
d. Stimulates the peristalsis.
e. Regulate the enzyme function of pancreas.
f. Converts ingested ferric ions (Fe3+) to ferrous ions
(Fe2+) to be used in hemoglobin production.
08. Gastric juice acidity. Kinds, methods of determination.
Free HCl, Bound HCl, Total HCl and total acidity… Ph. meter
and titrating by sodium hydroxide in presence of special
indicators.
Free HCl- 20-40mmol/l
Total acidity – 40-60 mmol/l
pH- 2 to 3.
09. Hypoaciditas, hyperaciditas, anaciditas.
Hypoaciditas- decrease of total acidity of gastric juice. Occurs
in chronic atrophic gastritis.
Hyperaciditas- increase in total acidity of gastric juice. Occurs
in ulcer disease, hyperacidic gastritis.
Anaciditas- absence of acidity in gastric juice. Occurs in
chronic atrophic gastritis & cancer of stomach.
010. Hypochlorhydria, hyperchlorhydria, achlorhydria.
Hypochlohydria- decrease of HCl content in gastric juice.
Occurs in chronic atrophic gastritis.
Hyperchlorhydria- increase of HCl content in gastric juice.
Occurs in ulcer disease, hyperacidic gastritis.
Achlorhydria- absence of hcl in gastric juice. In such
conditions, there is greater risk of infections of the
digestive tract (such as infection with Vibrio or
Helicobacter bacteria).
In diseases featuring excess vomiting, patients develop
hypochloremic metabolic alkalosis (decreased blood
acidity by H + and chlorine depletion).
011. Pathological components of gastric juice and their
determination.
a) Detection of the lactic acid: Lactic acid reacts with
Uffelman reagent (iron phenolate) producing iron lactate
of yellow-green color.
High amount of lactic acid can cause gastric carcinoma
(b) Detection of the blood in the gastric juice: Blood
peroxidase oxidizes benzidine in the presence of H2O2.
Oxidized benzidine has dark blue color.
It indicates ulcers or bleeding.
012. Mechanism of amino acid absorption.
Most proteins are absorbed in the form of amino acids.
However, small quantities of dipeptides and even tripeptides
are also absorbed, and extreme minute quantities of whole
proteins can be absorbed by the process of pinocytosis.
The mechanism by which amino acids are absorbed is
conceptually identical to that of monosacchides.
The lumenal plasma membrane of the absorptive cell bears
at least four sodium-dependent amino acid transporters -
one each for acidic, basic, neutral and amino acids.
These transporters bind amino acids only after binding
sodium.
This way of absorbtion nedeed enzyme Na+ -K+ -ATPase and
energy.
Thus, absorption of amino acids is also absolutely dependent
on the electrochemical gradient of sodium across the
epithelium.
Secondary active transport of amino acid providing the
energy for transport of the amino acid.
Absorption of amino acids through the intestine mucosa can
occur far more rapidly than protein can be digested in the
lumen of the intestine.
Amino acids and sometimes short oligopeptides are absorbed
by the secondary active transport Inhibits absorbtion of
amino acids - galactose and fructose.
Amino acids are transported via the blood to the cells of the
body.
013. Rotting of proteins in a large intestine, products.
The large intestine performs the following functions:
➢ reabsorbs water and maintains the fluid balance of the
body;
➢ absorbs certain vitamins;
➢ processes undigested material (fibre);
➢ stores waste before it is eliminated.
014. Deamination of amino acids, types.
Deamination - elimination of amino group from amino acid
with ammonia formation.
❖ Four types of deamination:
a. oxidative (the most important for higher animals)
b. reduction
c. hydrolytic
d. intramolecular
015. The role of enzymes, coenzymes, vitamins in process of
deamination.
016. Transamination of amino acids, mechanism,
Transamination - transfer of an amino group from an -
amino acid to an -keto acid (usually to -ketoglutarate)
Enzymes: aminotransferases (transaminases).
There are different transaminases
The most common:
❖ alanine aminotransferase (AlAT)
alanine + -ketoglutarate  pyruvate + glutamate
❖ aspartate aminotransferase (AsAT)
aspartate + -ketoglutarate  oxaloacetate + glutamate
Aminotransferases funnel -amino groups from a variety of
amino acids to -ketoglutarate with glutamate formation.
Glutamate can be deaminated with NH4 + release
Mechanism of transamination :
All aminotransferases require the prosthetic group pyridoxal
phosphate (PLP), which is derived from pyridoxine (vitamin
B6 ).
Ping-pong kinetic mechanism
➢ First step: the amino group of amino acid is transferred
to pyridoxal phosphate, forming pyridoxamine
phosphate and releasing ketoacid.
➢ Second step: -ketoglutarate reacts with pyridoxamine
phosphate forming glutamate

017. Role of enzymes and coenzymes in Transamination.

The most common:
alanine aminotransferase (AlAT)
alanine + -ketoglutarate  pyruvate + glutamate
aspartate aminotransferase (AsAT)
aspartate + -ketoglutarate  oxaloacetate + glutamate
Aminotransferases funnel -amino groups from a variety of
amino acids to -ketoglutarate with glutamate formation.
Glutamate can be deaminated with NH4 + release
018. Diagnostic role determination of AlAT and AsAT.
The concentration of transaminases in blood is used to
diagnose liver and heart disorders. Cause of AlAT level
increase in serum is liver damage (acute and chronic
hepatitis, when the cells of liver are destroyed).
Aspartate aminotransferase (AsAT) is abundant in heart
muscle, and increased blood levels of this enzyme indicate
damage (myocardial infarction).
019. Decarboxylation of amino acids.
Decarboxylation – removal of carbon dioxide from amino
acid with formation of biologically active amines.
Usually amines have high physiological activity (hormones,
neurotransmitters etc).
Enzyme: decarboxylases
Coenzyme – pyridoxal phosphate

➢ Compounds formed are:

a. Serotonin from tryptophan
b. Dopamine from Dopa
c. Histamine from Histidine
d. Gaba from Glutamate
020. Mechanism of decarboxylation reaction. Role of
enzymes and coenzymes.
Decarboxylation – removal of carbon dioxide from amino
acid with formation of biologically active amines.
Usually amines have high physiological activity (hormones,
neurotransmitters etc).
Enzyme: decarboxylases
Coenzyme – pyridoxal phosphate
021. Histamine and serotonin. From which amino acids are
formed? Role of Histamine and serotonin in organism.
a. Histamine from Histidine
b. Serotonin from tryptophan
➢ Histamine

Occurs in all tissues, but high in skin, Gastrointestinal tract,

lungs.
Found in mast cells or basophils at high conc.
Occurs as a component of venoms and in secretions from
insect stings.
It is a chemical messenger that mediates cellular response in
allergic and inflammatory reaction, gastric acid secretion,
and as a neurotransmitter.
Plays an imp role in gastric acid secretion.
➢ Serotonin
derived from tryptophan a brain chemical, is involved in
sleep, sensory perception, and the regulation of body
temperature and blood pressure.
Serotonin deficiency has been implicated in mental illness.
Treatment of mental depression can involve the use of drugs
that help maintain serotonin at normal levels by
preventing its breakdown within the brain.
 ➢ Histamine
Occurs in all tissues, but high in skin, Gastrointestinal tract,
lungs.
Found in mast cells or basophils at high conc.
Occurs as a component of venoms and in secretions from
insect stings.
It is a chemical messenger that mediates cellular response in
allergic and inflammatory reaction, gastric acid secretion,
and as a neurotransmitter.
Plays an imp role in gastric acid secretion.
➢ Serotonin
derived from tryptophan a brain chemical, is involved in
sleep, sensory perception, and the regulation of body
temperature and blood pressure.
Serotonin deficiency has been implicated in mental illness.
Treatment of mental depression can involve the use of drugs
that help maintain serotonin at normal levels by
preventing its breakdown within the brain.
022. Role of γ-aminobutyric acid (GABA) and dopamine in
organism.
➢ GABA
γ-aminobutyrate (GABA) is product of glutamate
decarboxylation.
It is the major inhibitory neurotransmitter in the central
nervous.
The term GABA refers to the simple chemical substance -
aminobutyric acid.
Its presence in the brain first was reported in 1950 (Roberts
and Frankel)
➢ Dopamine
Dopamine is precursor of chemical L-DOPA.
Dopamine is a neurotransmitter released by the brain that
plays a number of roles in humans and other animals.
Some of its notable functions are in:
• movement
• memory
• pleasurable reward
• behavior and cognition
• attention
• inhibition of prolactin production
• sleep
• mood
• learning
 Excess and deficiency of Dopamine results in Parkinson's
disease, a degenerative neurological disease.
Administration of dopamine to a patient does not stop the
symptoms of this disease, because dopamine in the blood
cannot cross the blood-brain barrier. The drug L-dopa, which
can pass through the blood-brain barrier, does give relief
from Parkinson's symptoms.
023. Sources of ammonia in organism.
Ammonia-(NH3) is a toxic compound that needs to be
detoxified and eliminated from the body.

024. Transport form of ammonia from peripherial tissue.

Three transport forms of ammonia from peripheral tissues to
liver:
 a. Glutamate- All tissues
b. Glutamine- Brain
c. Alanine- Muscle
025. Biosynthesis of urea, localization of this process.
80% of the excreted nitrogen is in the form of urea which is
also largely made in the liver.
Localisation of urea cycle - between the mitochondrial matrix
and the cytosol. The series of reactions that form urea is
known as the Urea Cycle.
In 1932 Krebs and Henseleit descoverd urea cycle.
026. Enzymes and coenzymes of urea cycle.

027. Diagnostic significance determination of urea in blood

and urine.
➢ In Blood:
 Normal level- 15 to 45 mg/dl
Uremia or azotemia is increased blood urea level due to renal
failure.
High value of blood uea indicates significant reduction in GFR
and kidney disease.
➢ In Urine:
In normal conditions 25-30 g of urea is excreted per day .
Elevated urea levels in the urine can be caused by high fever,
malignant anemia, phosphorus poisoning , and intensive
protein decomposition in the organism.
Decreased urea levels in the urine can be caused by liver
diseases, kidney insufficiency, and acidosis.
028. Uremia, causes, consequences for organism.
a raised level in the blood of urea and other nitrogenous
waste compounds that are normally eliminated by the
kidneys.
029. Primary enzyme pathologies of cyclic and branched
amino acids, their clinical and laboratory diagnostics.
Maple syrup urine disease - the disorder of the oxidative
decarboxylation of -ketoacids derived from valine,
isoleucine, and leucine caused by the missing or defect of
branched-chain dehydrogenase.
The levels of branched-chain amino acids and corresponding
-ketoacids are markedly elevated in both blood and
urine. The urine has the odor of maple syrup
The early symptoms:
 lethargy
 ketoacidosis
 unrecognized disease leads to seizures, coma, and death
 mental and physical retardation
030. Glycogenic and ketogenic amino acids.
➢ Amino acids that are degraded to citric acid cycle
intermediates can serve as glucose precursors and are
called glucogenic.
A glucogenic amino acid is an amino acid whose carbon-
containing degradation product(s) can be used to produce
glucose via gluconeogenesis.
➢ Amino acids that are degraded to acetyl CoA or
acetoacetyl CoA can contribute to the formation of fatty
acids or ketone bodies and are called ketogenic.
A ketogenic amino acid is an amino acid whose carbon-
containing degradation product(s) can be used to produce
ketone bodies.

031. The effect of hormones of pituitary gland, pancreas

(insulin, glucagon, somatostatin, lipocain).
Insulin:
•increases the permeability of cell membranes for amino
acids;
•activates synthesis of proteins and nucleic acids;
•inhibits the conversion of amino acids into carbohydrates.
Glucagon:
•stimulates the conversion of amino acids into
carbohydrates.
Somatotropic hormone (STH, growth hormone): -
stimulates the passing of amino acids into the cells; -
activates the synthesis of proteins, DNA, RNA.
Somatostatin
Inhibits secretion of insulin and glucagon
• Inhibits secretion of STH and TTH
• Inhibits secretion of local hormones of intestine.
Lipocain
• Activates the synthesis of phospholipids in liver
• Stimulates the action of lipotropic factors
• Activates the oxidation of fatty acids in liver

032. The effect of hormones of thyroid, sex and adrenal

glands on protein metabolism.
Thyroxine and triiodthyronine:
- in normal concentration stimulate the synthesis of proteins
and nucleic acids; - in excessive concentration activate the
catabolic processes.
Sex hormones:
•stimulate the processes of protein, DNA, RNA synthesis;
•cause the positive nitrogenous balance
Epinephrine: - activates the protein decomposition
Glucocorticoids:
•stimulate the catabolic processes (protein decomposition)
in connective, lymphoid and muscle tissues and activate
the processes of protein synthesis in liver;
•stimulate the activity of aminotransferases;
•activate the synthesis of urea.
033. Structure and biological role of nucleotides.
Nucleotides are organic molecules that serve as the
monomers of nucleic acids like DNA and RNA.
The building blocks of nucleotides are composed of a
nitrogenous base, a five-carbon sugar (ribose or
deoxyribose and phosphate group).
034. The hydrolysis of nucleoproteins and nucleic acids in
the digestive tract and tissues.

035. The decomposition of purine nucleotides to the end

products.
The end product of purine catabolism in man is uric acid. Uric
acid is formed primarily in the liver and excreted by the
kidney into the urine.
Nucleotides to Bases
Guanine nucleotides are hydrolyzed to the nucleoside
guanosine which undergoes phosphorolysis to guanine and
ribose 1-P.
Man's intracellular nucleotidases are not very active toward
AMP, however.
Rather, AMP is deaminated by the enzyme adenylate (AMP)
deaminase to IMP.
In the catobilsm of purine nucleotides, IMP is further
degraded by hydrolysis with nucleotidase to inosine and
then phosphorolysis to hypoxanthine.
Adenosine does occur but usually arises from S-
Adenosylmethionine during the course of
transmethylation reactions.
Adenosine is deaminated to inosine by an adenosine
deaminase.
Deficiencies in either adenosine deaminase or in the purine
nucleoside phosphorylase lead to two different
immunodeficiency diseases by mechanisms that are not
clearly understood.
With adenosine deaminase deficiency, both T and B-cell
immunity is affected.
The phosphorylase deficiency affects the T cells but B cells
are normal. In September, 1990, a 4 year old girl was
treated for adenosine deaminase deficiency by genetically
engineering her cells to incorporate the gene.
The treatment,so far, seems to be successful. Whether or not
methylated purines are catabolized depends upon the
location of the methyl group. If the methyl is on an -NH2, it
is removed along with the -NH2 and the core is
metabolized in the usual fashion.
If the methyl is on a ring nitrogen, the compound is excreted
unchanged in the urine.
Bases to Uric Acid
Both adenine and guanine nucleotides converge at the
common intermediate xanthine.
Hypoxanthine, representing the original adenine, is oxidized
to xanthine by the enzyme xanthine oxidase. Guanine is
deaminated, with the amino group released as ammonia,
to xanthine.
If this process is occurring in tissues other than liver, most of
the ammonia will be transported to the liver as glutamine
for ultimate excretion as urea.
Xanthine, like hypoxanthine, is oxidized by oxygen and
xanthine oxidase with the production of hydrogen
peroxide. In man, the urate is excreted and the hydrogen
peroxide is degraded by catalase.
Xanthine oxidase is present in significant concentration only
in liver and intestine. The pathway to the nucleosides,
possibly to the free bases, is present in many tissues.
036. Uric acid – final excretory product of purine
metabolism in humans.
0.5-1 g of uric acid is formed daily in the organism and
exreated with urine. Normal concentration of uric acid in
blood:
in man – 0.24-0.50 mmol/L
in women – 0,16 – 0,40 mmol/l
Uric acid – poorly soluble in water

037. Gout: symptoms, treatment.

High levels of uric acid is called hyperuricemia and can lead
to gout.
➢ accumulation salts of uric acid in joints
➢ accumulation of uric acid salts in soft
tissue, under skin
038. Lesch-Nyhan syndrome: symptoms, treatment.
Lesch-Nyhan syndrome –
inherited diseases accompanied with primary hyperuricemia
and crystallization of uric acid and salts in joints, cartilages
and kidneys.
Salts of uric acid – urates.
Symptoms: -joints inflammation,
acute pain
-renal stones
-tophuses.
Uric acid crystal deposits in the joint cause inflammation of
the joint leading to pain, redness, heat, and swelling.
039. The synthesis of purine nucleotides.
Ribosphosphate is formed in pentose-phosphate pathway
from glucose
Purine ring is synthesized on ribose-5- phosphate by the way
of gradual adding of nitrogen and carbon atoms and
cyclization.
The way of biosynthesis consist of 11 reactions.
Two ways of biosynthesis:
-de novo – formation of purine nucleotides from simple
acyclic precursors (in liver)
-salvage (reserve) pathway – using of purine bases formed in
the decomposition of nucleotides (in the out-of-liver
tissues)

040. Precursors of the purine ring.

• Glycine
• Glutamine
• Aspartate
• Formate
• CO2

041. The structure and biological role of pyrimidine

nucleotides.
Pyridmidines have only a sixmembered nitrogen-containing
ring.
Three nucleobases found in nucleic acids - cytosine (C),
thymine (T), and uracil(U), are pyrimidine derivatives:

042. The decomposition of pyrimidine nucleotides to the

end products
CMP and UMP are degraded to β-alanine and NH3 and CO2 .
TMP degraded to βaminoisobutyrate.
The β-alanine and β-aminoisobutyrate serve as -NH2 donors
in transamination of αketoglutarate to glutamate.
NH3 and CO2 used in biosynthesis of urea.
β-alanine – structural component of CoA.
β-aminoisobutyrate convert into succinil CoA.
043. The synthesis of pyrimidine nucleotides. Precursors of
the pyrimidine rings.
Enzyme names:
1. Carbamoyl phosphate synthetase II
2. aspartate transcarbamylase
3. dihydroorotate dehydrogenase
4. orotate phosphoribosyltransferase
5. orotidine-5'-phosphate carboxylase
Pyrimidine synthesis begins with carbamoyl phosphate
synthesized in the cytosol of those tissues capable of
making pyrimidines (highest in spleen, thymus, GItract and
testes).
Carbamoyl phosphate synthetase II (CPS II) prefers glutamine
to free ammonia.
Carbamoyl phosphate condenses with aspartate in the
presence of aspartate transcarbamylase to yield N-
carbamylaspartate which is then converted to
dihydroorotate.
Oxidation of the ring by a complex, poorly understood
enzyme produces the free pyrimidine, orotic acid.
This enzyme is located on the outer face of the inner
mitochondrial membrane, in contrast to the other
enzymes which are cytosolic.
Orotic acid is converted to its nucleotide with
phosphoribosyltransferase. OMP is then converted
 sequentially - not in a branched pathway - to the other
pyrimidine.
Decarboxylation of OMP gives UMP.
O-PRT and OMP decarboxylase are also a multifunctional
protein.
In reaction amination UMP convert to CMP
044. Orotaciduria: symptoms, treatment.
Orotic aciduria is an autosomal recessive disorder of
pyrimidine synthesis by def. of enzyme oratare-
phosphoribosyl-transferase and decarboxylase.
Symptoms:
–excess of orotic acid and its excretion with urine (1.0-1.5 g)
-mental and physical retardation
-megaloblastic anemia
Treatment:
Taking of uridin during the whole life
045. Diagnostic importance of the uric acid analysis.
046. Nucleic acids: kinds, structure, functions.
➢ Nucleic acids - are large organic macromolecules that store
genetic information and enable protein production.
Nucleic acids found in the chromosomes and nucleus of the
cells.
They are strong acids – optimal pH – 7
➢ Two types of nucleic acids – DNA and RNA
Functions of nucleic acid:
➢ The main functions - is store and transfer genetic
information.
➢ To use the genetic information to direct the synthesis of
new proteins.
➢ The DNA is the storage for place of genetic information in
the cell.
➢ DNA controls the synthesis of RNA in the cell.
➢ The nucleotide ATP (adenosine triphosphate), which is
closely related to DNA and RNA, is the short-term energy
storage for all life processes.
➢ RNA also directs the production of new protein by
transmitting genetic information to the protein building
structures.
047. General postulate of molecular biology.
The central dogma of molecular biology is an explanation of
the flow of genetic information within a biological system.
It is often stated as "DNA makes RNA and RNA makes
protein"
There are three types transmission of genetic information:
1. Replication
2. Transcription
3. Translation
048. Replication of DNA: components, mechanisms.
Components which are necessary for replication - named -
replisom
• Enzymes (most important – DNA-dependent DNA
polymerase)
• Protein factors
• Parental DNA
• ATP, GTP, ТТP, CТP
• Ions Mg і Zn
➢ In eukaryotes the replication begins in many points
simultaneously
• V-shape – replication forks - the point of the beginning of
replication
• Helicase – enzyme untwisting the double strand, during
untwisting (used 2 mol. of ATP)

DNA Replication
The prokaryotic replication process contains several basic
steps, each of which requires certain enzyme activities:
1. DNA uncoiling. As their name implies, the helicases are
ATP-requiring enzymes that catalyze the unwinding of
duplex DNA.
2. Primer synthesis. The formation of short RNA segments
called primers, which are required for the initiation of DNA
replication, is catalyzed by primase.
3. DNA synthesis. The synthesis of a complementary DNA
strand by creating phosphodiester linkages between
nucleotides base paired to a template strand is catalyzed
by large multienzyme complexes referred to as the DNA
polymerases.
DNA polymerase III (pol III), the major DNA-synthesizing
enzyme, is composed of at least ten different subunits.
DNA polymerase I (pol I) is a DNA repaer enzyme. (Pol I is
also believed to play a role in the timely removal of RNA
primer.)
The function of DNA polymerase II (pol II) is not understood.
In addition to a 5'→3' polymerizing activity, all three
enzymes possess a 3'→5' exonuclease activity (An
exonuclesse is an enzyme that removes nucleotides from
an end of a potynucleotide strand.) Pol I also possesses a
5'→3' exonuclease activity.
4. Joining of DNA fragments. Discontinuous DNA synthesis
(described below) requires an enzyme, referred to as a
ligase, that joins the newly synthesized segments.
5. Supercoiling control. The tangling of DNA strands, which
can prevent further unwinding of the double helix, is
prevented by the DNA topoisomerases.
Tangling is a very real possibility, since the double helix
unwinds rapidly (as many as 50 revolutions per second
during bacterial DNA replication).
Topoisomerases are enzymes that alter the linking number of
closed duplex DNA molecules.
The terms "topoisomerase" and "topoisomers" (circular DNA
molecules that differ only in their linking numbers) are
derived from "topology," a form of mathematics that
investigates the properties of geometric structures that do
not change with bending or stretching.
Replication ends when the replication forks collide on the
other side of circular chromosome.
The subsequent separation of the two daughter DNA
molecules is not understood, although a type II
topoisomerase is believed to be involved.
049. The principal and mechanism of transcription.
NECESSARY COMPONENTS
•DNA matrix
•RNA-polymerase
•АТP, GТP, CТP, UТP
•Мg ions
RNA Polymerase
There are 3 RNA-polymerases in eukaryotes (for mRNA,
rRNA, tRNA)
• RNA pol is core of a larger transcription complex
• Complex assembles at one end of a gene (promoter) when
transcription is initiated – transcription initiation
• DNA is continuously unwound as RNA pol catalyzes a
processive elongation of RNA chain
The Chain Elongation Reaction
• Mechanism almost identical to that for DNA polymerase
• Growing RNA chain is base-paired to DNA template strand
• Incoming ribonucleotide triphosphates (RTPs) form correct
H bonds to template
• New phosphodiester bond formed
• Direction 5’-3’
• Speed - 30-85 nucleotides/sec
 Transcription Termination
•Only certain regions of DNA are transcribed
•Transcription complexes assemble at promoters and
disassemble at the 3’ end of genes at specific termination
sequences.
050. Modification of RNA. Inhibitors of transcription
(proteins, antibiotics).
During transcription formed 3 types of RNA.
Mrna- messenger rna
• Encodes message from DNA to ribosomes
• Rapidly degraded by nucleases
Trna- transfer rna
• Carries amino acids to translation machinery
• Very stable molecules
Rrna- Ribosomal rna
• Makes up much of the ribosome
• Very stable, majority of cellular RNA
051. Genetic code, properties.
sequence of mononucleotides in mRNA that specifies the
sequence of amino acids in peptide chain
PROPERTIES
1. Unambiguous. In any organism each codon corresponds to
only one amino acid.
2. Code is degenerate. There are multiple codons for most
amino acids.
3. Universal. Codons are the same for all organism.
4. Without punctuation. There are no punctuations between
trinucleotides.
5. Nonoverlapping. Codons do not overlap each other.
052. Codons and anticodons.
CODON – mRNA triplet base sequence responsible for 1
amino acid
ANTIcodon- triplet in trna that can complemtary bind to
codon of mRNA.
053. Ribosomal protein synthesis system, components.
Components
• Codon
• Anticodon (aminoacyl-tRNA)
• Enzymes
• Amino acid
• ATP
1.Activation
• Synthetase catalysis the formation of aminoacyl-1-AMP
• Activating the amino acid through formation of high energy
mixed anhydride bond to form pyrophosphate
2.tRNA linkage
• Specific tRNA binds to actie site of synthetase through an
ester line
• This drives peptide bond formation Amino acid +ATP
>aminoacyl-tRNA +AMP +PP

054. Stages and mechanisms of translation.

STAGES OF TRANSLATION
1. Recognition
2. Initiation
3. Elongation
4. Termination
The translation of a genetic message into the primary
sequence of a polypeptide can be divided into three
phases: initiation, elongation, and termination.
1. Initiation. Translation begins with the formation of an
initiation complex. In prokaryotes this process requires
three initiation factors (IFs). IF-3 has previously bound to
the 30S subunit, thereby preventing it from binding
prematurely to the 50S subunit. As an mRNA binds to the
30S subunit, it is guided into a precise location, so that the
initiation codon AUG is correctly positioned. Each gene on
a polycistronic mRNA possesses its own initiation codon.
The translation of each gene appears to occur
independently, that is, translation of the first gene may or
may not be followed by the translation of subsequent
genes.
2. Elongation. It is during the elongation phase that the
polypeptide is actually synthesized according to the
specifications of the genetic message. Elongation, the
phase in which amino acids are incorporated into a
polypeptide chain, consists of three steps: (1) positioning
of an aminoacyl-tRNA in the A site, (2) peptide bond
formation, and (3) translocation.
3.Termination. The termination phase begins when a
termination codon (UAA, UAG, or UGA) enters the A site.
Three releasing factors (RF-1, RF-2, and RF-3) are involved
in termination. The codons UAA and UAG are recognized
by RF-1, whereas UAA and UGA are recognized by RF-2.
055. Post translation modification of proteins.
Post-translational modification (PTM) refers to the covalent
and generally enzymatic modification of proteins following
protein biosynthesis.
Proteins are synthesized by ribosomes translating mRNA into
polypeptide chains, which may then undergo PTM to form
the mature protein product. 1. Removing of methionine
(formylmethionine)
2. Formation of disulfide and other bonds (secondary,
tertiary structures)
3. Proteolytic cleavage
4. Modification of amino acid residues:
- Hydroxylation
- Glycosilation
- Phosphorilation
5. Joining of prosthetic groups or cofactors 6. Formation of
the quaternary structure
056. Inhibitors of protein synthesis.
 ➢ Tetracycline: inhibits binding of aminoacyl
t-rnas to ribosomes and thereby blocks
continued translation.
➢ Streptomycin: interferes with normal
pairing between aminoacyl t-rnas and
message codons, causing misreadings and
thereby produce aberrant proteins.
➢ Erythromycin: binds to specific site on 23 S
RNA and blocks elongation by interfering
with translocation step
➢ Chloramphecinol: Blocks elongation, by
acting as competitive inhibitor for the
peptidylytransferase complex
➢ Puromycin: Causes premature chain
termination.
057. Hormones as biological regulators. Hormonoids
(histohormones).
1. Growth and differentiation of cells, tissues and organs.
These processes include cell proliferation, embryonic
development, and sexual differentiation.
2. Metabolic pathways The main processes to hormonal
regulation are the uptake and degradation of storage
substances (glycogen, fat), metabolic pathways for
biosynthesis and degradation of central metabolites
(glucose, fatty acids, etc.), and the supply of metabolic
energy.
Digestive processes are usually regulated by locally acting
peptides (paracrine), but mediators, biogenic amines, and
neuropeptides are also involved.
Maintenance of ion concentrations (homeostasis)
Concentrations of Na+, K+, and Cl– in body fluids, and the
physiological variables dependent on blood pressure, are
subject to strict regulation. The principal site of action of
the hormones involved is the kidneys, where hormones
increase or reduce the resorption of ions and recovery of
water. The concentrations of Ca2+ and phosphate, which
form the mineral substance of bone and teeth, are also
precisely regulated.
Hormonoids (tissue hormones, histohormones) - organic
trace substances produced by different cells of different
tissues (not by specific glands) that regulate metabolism
on the local level (some hormonoids are produced in the
blood too (serotonin, acetylcholine). Acetylcholine is a
neurotransmitter. Releases chemicals into the brain and
plays a role in normal brain functions such as sleep. Also, it
deals with attention, learning, and memory skills. The
mechanisms that the transmitter controls was a mystery
until now. Scientist now know that acetycholine deals with
communication between neurons. Located in the
prefrontal cortex.
Heparin, is an naturally-occurring anticoagulant (blood
thinner) produced by basophils and mast cells that
prevents the formation of blood clots.
Heparin is used to treat and prevent blood clots in the veins,
arteries, or lung. It is also used before surgery to reduce
the risk of blood clots.
Secretin is a hormone that both controls the environment in
the duodenum by regulating secretions of the stomach and
pancreas, and regulates water homeostasis throughout the
body.
Secretin regulates the pH within the duodenum by inhibiting
gastric acid secretion by the parietal cells of the stomach,
and by stimulating bicarbonate production by the
centroacinar cells and intercalated ducts of the pancreas.
Secretin stimulates pepsin secretion from chief cells, which
can help break down proteins in food digestion. It
stimulates release of glucagon, pancreatic polypeptide and
somatostatin.
Histamine, an important mediator (local signaling substance)
and neurotransmitter, is mainly stored in tissue mast cells
and basophilic granulocytes in the blood.
It is involved in inflammatory and allergic reactions.
Histamine is found in plant and animal tissue and is
released from mast cells as part of an allergic reaction in
humans.
Release of histamine stimulates gastric secretion and causes
dilation of capillaries, constriction of bronchial smooth
muscle, and decreases blood pressure
Gastrin
It is a peptide hormone.
Stimulates secretion of gastric acid by parietal cells of
stomach.
Aids in gastric moeity
058. Endocrine glands. Classification of hormones.
Endocrine Glands:
1. Hypothalamus
2. Pituitary
3. Epiphysis
4. Thymus
5. Thyroid gland
6. Parathyroid glands
7. Langergans’ islands of pancreas
8. Epinephrine glands
9. Sex glands
Classification of hormones according to chemical nature
1. Proteins: hormones of anterior pituitary (except ACTH),
insulin, parathyroid hormone.
2. Peptides: ACTH, calcitonin, glucagon, vasopressin,
oxytocin, hormones of hypothalamus (releasing factors
and statins).
3. Derivatives of amino acids: catecholamins (epinephrine
and norepinephrine), thyroxin, triiodthyronin, hormones of
epiphysis.
4. Steroid (derivatives of cholesterol): hormones of the cortex
of epinephrine glands, sex hormones.
5. Derivatives of polyunsaturated fatty (arachidonic) acids:
prostaglandins.
059. Receptors of hormones.
• Hormones act on specific cells that called target cells. The
target cells has a specific protein molecule, called a receptor.
Two groups:
• placed on the surface of membrane – peptide and protein
hormones, prostaglandins
• placed inside the cells (cytoplasm, nucleus) – steroid and
Thyroid hormones
060. Hormones of hypothalamus (releasing and inhibitory
factors), structure, role.
Releasing factors (liberins) stimulate secretion of pituitary
hormones;
statins - inhibit.
•somatoliberin,
•somatostatin,
•prolactostatin,
•melanostatin
•thyroliberin,
•corticoliberin,
•foliliberin,
•prolactoliberin,
•luteinising-hormone liberin,
•melanoliberin
Secretion of liberins and statins by hypothalamus is carried
out
1) the effect of nervous impulses and
2) as result of the change of concentrations of certain
hormones in blood (feedback regulation).
061. Hormones of anterior pituitary (7 hormones).
062. Why hormones of anterior pituitary are called “tropic”
hormones?
Tropic – because stimulate functions of peripheral endocrine
glands
063. Somatotropic hormone: nature, structure, effect on
protein, carbohydrate and lipid metabolism.
Chemical nature – simple protein
It is secreted continuously during the whole life
Secretion is stimulated by somatoliberin, is inhibited by
somatostatin
Main function – stimulate somatic growth of organs and
tissues, particularly bones, cartilages, muscles.
The effect of STH on the protein metabolism
➢ Promotes the entrance of AA into cells,
➢ Inhibits catabolism of proteins and AA
➢ Activates the synthesis of proteins, DNA,
RNA.
The effect of STH on the carbohydrate metabolism
➢ Antiinsulin hormone – activates insulinase of liver
➢ Activates the exit of glucose from liver
➢ Inhibits the conversion of glucose into fat
The effect of STH on lipid metabolism
➢ Stimulates the decomposition of lipids (lipolisis)
➢ Stimulates the oxidation of fatty acids.
064. Adrenocorticotropic hormone: chemical structure,
biological role.
Chemical nature – polypeptide
Controls the cortex of epinephrine gland where cortisol is
produced:
-promotes the increase of cholesterol content in epinephrine
glands cortex and its conversion into corticosteroids;
-activates the passing of glucose into epinephrine glands and
pentose phosphate cycle (NADPH synthesis)
-has melanocyte stimulating activity
065. Follicle stimulating hormone and Luteinizing hormone:
chemical structure, biological role.
Follicle-stimulating hormone
Chemical nature – protein (glycoprotein)
Function: stimulates the function of follicles in women and
spermatogenesis in men
Luteinizing hormone
Chemical nature – protein (glycoprotein)
Function: stimulates the follicular growth and conversion of
the follicle into a corpus luteum in women and secretion of
testosterone in men
066. Prolactin and Lipotropic hormone: chemical structure,
biological role.
Prolactin
Chemical nature – protein
Functions:
-During and following pregnancy, prolactin, stimulates breast
development and milk production.
-provides the body with sexual gratification;
-stimulates the function of corpus luteum (progesterone
secretion);
-stimulates the growth of tissue of prostatic gland in men;
-responsible for the mother instinct
Lipotropic hormone
Chemical nature – simple proteins
Functions:
- mobilization of lipids from depot;
- melanocyte stimulating function;
- decrease Ca in blood
067. Vasopressin: chemical structure, biological role.
Chemical nature – peptide
Function:
➢ Decreased urine production
➢ Decrease sweating
➢ Increase BP by retaining water
➢ increases the reabsorption of water in kidneys;
➢ contractions arterioles and capillaries
068. Oxytocin: chemical structure, biological role, using in
medical practice.
Chemical nature – peptide
Functions:
stimulates the contraction of smooth muscles (of uterus
during labor)
-stimulates milk secretion (contraction of muscle fibers
around mammary alveoli)
Using:
-for labor stimulation;
-to stop after labor hemorrhage;
-for stimulation of milk secretion
069. Iodine containing hormones of thyroid gland. Chemical
structure.
Iodine containing hormons:
thyroxin (tetraiodthyronin) and triiodthyronin –
derivatives of aminoacid - tyrosine;
070. Effect of thyroxine and triiodthyronine on protein
metabolism.
In physiological concentration iodine containing hormones
stimulate synthesis of proteins, nucleic acids. In the
increased concentration activate the protein
decomposition.
071. Disorders of metabolic processes at hypothyroidism.
Hypofunction of gland – endemic goiter (occurs in the deficit
of iodine in water, soil, air )
•Decrease of basic metabolism
•Decrease of body temperature
Hypofunction in childhood - cretinism
•Growth inhibition
•Unproportional body development
•Disorders of mental development
Hypofunction in adults – mixedema
•Edema of mucosa
072. Disorders of metabolic processes at hyperthyroidism.
Hyperfunction of gland – diffuse toxic goiter (thyrotoxicosis,
Graves disease)
073. Calcitonin: chemical structure, biological role.
Calcitonin – peptide (32 aminoacid residues).
Hormone calcitonin is produced by the parafollicular cells of
the thyroid gland, has the opposite effect on blood calcium
levels as PTH.
Calcitonin decreases blood calcium levels by inhibiting
osteoclasts, stimulating osteoblasts, and stimulating
calcium excretion by the kidneys.
This results in calcium being added to the bones to promote
structural integrity.
Calcitonin is most important in children (when it stimulates
bone growth), during pregnancy (when it reduces maternal
bone loss) and during prolonged starvation (because it
reduces bone mass loss).
Calcitonin decreases the renal tubular capacity for phosphate
reabsorption
074. Parathyroid hormone: chemical structure, biological
role.
Parathyroid hormone – protein (84 aminoacid residues)
- Affects the metabolism of Са and Р
- Promotes moving of Са2+ from bones into blood
- Inhibits reabsorbtion of Р in kidneys (decreases the content
of Р in blood due to its excretion with urine)
- Stimulates the absorption of Ca in the intestine
- Activate formation of active form of vitamin D in kidney

075. Hormones of pancreas. Insulin: chemical structure,

proinsulin, regulation of insulin production.
➢ Nature – protein (51 АA)
➢ Is formed from proinsulin by proteolisis
➢ Contains zinc
Secreted by beta cells of pancreas.
➢ Regulation of the synthesis:
- Glucose concentration in blood
- Other hormones (somatostatin)
- Sympathetic and parasympathetic nervous system
076. Effect of insulin on carbohydrate and lipid metabolism.
The effect on carbohydrate metabolism
•Increases the permeability of membranes for glucose
•Activates glucokinase (hexokinase) in glycolysis
•Activates TAC (citrate synthase)
•Activates PPC (G-6-PDH)
•Activates glycogen synthase
•Activates pyruvate- and alpha-кetoglutarate dehydrogenase
•Inhibits gluconeogenesis
•Inhibits the decomposition of glycogen (glucose-6-
phosphatase)
Effect on the lipid metabolism
Activates of the lipids synthesis
•Promotes the saving of fats activating the decomposition of
carbohydrates
•Inhibits gluconeogenesis
077. Glucagon: chemical structure, biological role.
 Nature – polypeptide
Functions
 Activates the decomposition of glycogen in liver
 Activates gluconeogenesis
 Inhibits glycolysis
 Activates lipolysis
078. Somatostatine: chemical structure, biological role.
Nature – peptide
Functions:
• Inhibits secretion of insulin and glucagon
• Inhibits secretion of STH and TTH
• Inhibits secretion of local hormones of intestine
079. Hormones of adrenalmedulla – catecholamines:
chemical structure, physiological role.
Epinephrine, norepinephrine and DOPA
All catecholamines are synthesized from the amino acid -
tyrosine according to the following sequence:
tyrosine → dopa (dihydroxyphenylalanine) → dopamine →
norepinephrine (noradrenaline) → epinephrine
(adrenaline)
Catecholamines are synthesized in the brain, adrenal medulla
and by some sympathetic nerve fibres.
Functions:
Stress hormones.
Contraction of vessels, increase the blood pressure,
accelerate pulse.
Contraction of uterus muscles.
Epinephrine relaxes the muscles of bronchi and intestine.
080. Glucocorticoids: chemical structure, representatives.
Chemical nature – steroid
Most important: corticosteron, cortisol, hydrocortison
081. Mineralocorticoids: chemical structure, representative.
Steroid
The most important hormone: aldosteron
082. Sex hormones: kinds, structure, place of synthesis.
They are steroids.
• Are synthesized in: -
sex glands
-placenta
-cortex of epinephrine glands
A little amount of female sex hormones is formed in male
organism and vice versa.
• Female – estrogens, progesteron.
• Male – androgens.
083. Estrogenes: representatives, biological role.
Nature: steroids
• Estradiol – is formed in follicles of ovarium
• Estron and estriol – are formed in liver and placenta in
the metabolism of estradiol
Functions of estrogens
Development of the female reproductive system organs
Ability to fertility in reproductive period
Biochemical functions of estrogens
Anabolic action on the tissues of reproductive organs
Inhibit the exit of Ca from bones (osteoporosis in
menopause)
084. Prostaglandins: chemical structure, functions.
• Prostaglandins are a group of lipid made at site of tissue
damage or infection that are involved in dealing with
injury or illness.
• They control processes such as inflammation, blood
flow, formation of blood clots and induction of labour.
• Prostaglandins are involved in several other organs such
as the gastrointestinal tract (inhibit acid synthesis and
increase secretion of protective mucus), increase blood
flow in kidneys, and leukotriens promote constriction of
bronchi associated with asthma.
• The precursor of prostaglandins is arachidonic acid
• Half life is 30 s.
085. Renin-angiotensin system: functions.
• Renin-angiotensin system or renin– angiotensin–
aldosterone system is a hormone system that regulates
blood pressure and fluid balance.
• Renin - enzyme that synthesized in juxtaglomerular cells
of the kidneys and secrete directly into the circulation
blood.
• In the case of hypovolemia (decrease in blood volume)
and low blood pressure the kidneys cells of the renal
juxtaglomerular apparatus begin the synthesis of
protein renin.
• Renin acts on angiotensinogen (which is made in the
liver).
• As result angiotensin-I is formed.
 • Angiotensin I is subsequently converted to angiotensin II
by the enzyme angiotensin-converting enzyme (ACE)
found in the lungs.
• Angiotensin-II causes 2 effects: - narrows the vessels and
increases the blood pressure; - stimulates the secretion
of aldosterone.
• Aldosterone causes the renal tubules to increase the
reabsorption of sodium and water into the blood, while
at the same time causing the excretion of potassium (to
maintain electrolyte balance).
• This increases the volume of extracellular fluid in the
body, which also increases blood pressure

1. Concepts: "vitamin", "provitamin", "avitaminosis",

"hypervitaminosis" and "hypovitaminosis". Classification
of vitamins.
Answer:
• Vitamins – low molecular weight organic compounds
that have different chemical structure and are not
synthesized or are synthesized in small amount in the
human organism, have marked biological effect and are
necessary components of diet.
• Hypovitaminosis – decrease of vitamin amount in the
organism
• Hypervitaminosis – increase of vitamin amount in the
organism
• Avitaminosis – lack of vitamin in the organism
• Provitamins - a precursor of a vitamin convertible into
the vitamin in an organism
• Antivitamins - a substances that inactivates or inhibits
synthesis of a vitamins.
There are two major classes of Vitamins:
➢ Water Soluble:
C
P
H
B complexes
➢ Fat Soluble
A
D
E
K
F
2. Chemical and physiological name, coenzymes, biological
role of vitamins B1.
Answer:
➢ Chem name: thyamine
➢ Phy name: antineuritic
➢ ТМP, ТDP and ТТP are coenzymes of:
-pyruvate- and
alpha-ketoglutarate dehydrogenase
-transketolase
➢ Functions: Essential for nerve and muscle function and
metabolism of carbs and amino acids.
3. Manifestations of hypovitaminosis, nature sources and
day requirement of vitamins B1.
Answer:
➢ Sources are meats, legumes, wheat germ, cereals, lean
prok, yeast.
➢ Daily requirement: 1-3 mg
Chronic deficiency of thiamine
Often found in -poor countries -alcoholics
Two types: dry and wet
Dry: disseminated polyneuritis, partial paralysis, weakness
and pain in the limbs, atrophy, loss of weight, impaired
sensory perception
Wet: heart failure, edema, dystrophy of myocardium
Wernicke-Korsakoff syndrome: hemorrhage in CNS.
Mental disorders, amnesia, encephalopathy, psychosis
➢ Beri beri is caused due to b1 def.

4. Chemical and physiological name, coenzymes, biological

role of vitamins B2.
Answer:
➢ Chem name: Riboflavin
➢ Phy name: Growth vitamin
➢ Coenzymes: FMN & FAD
➢ Role: Are necessary for the action of more than 30
enzymes
 ➢ – oxido-reductases (оxidation-reduction reactions)
➢ -AA deamination (оxidases of AA)
➢ -pyruvate dehydrogenase and alpha-ketoglutarate
complexes
➢ -succinate dehydrogenase (Krebs cycle)
➢ -fatty acids oxidation (acyl CoA dehydrogenase)
➢ -uric acid formation (xanthine oxidase)
-electron transport in respiration chain

5. Manifestations of hypovitaminosis, nature sources and

day requirement of vitamins B2.
Answer:
Hypovitaminosis – disorders of the processes of biological
oxidation
Symptoms: cracks at the corner of mouth
Dermatitis
Glossitis
Ceratitis
Blepharitis
Conjunctivitis
Sources: cereals, nuts, milk, eggs, green leafy vegetables,
lean meat
Daily req.- 1-3 mg
6. Chemical and physiological name, coenzymes, biological
role of vitamin B3.
Answer:
➢ Chem name: pantothenic acid
➢ Phys name: antidermatitic
➢ Coenzymes: coA &
Phosphopantothenate
➢ Biological Role:
-oxidative decarboxilation of pyruvate and alpha-
ketoglutarate –
transport of the fatty acids residues
-synthesis of purine nucleotides
-activation of fatty acids durind beta- oxidation of fatty
acids
-phosphopantothenate is a constituent of multienzyme
complex
– fatty acids synthase
-cholesterol synthesis
-ketogenesis

7. Manifestations of hypovitaminosis, nature sources and

day requirement of vitamin B3.
Answer:
➢ Hypovitaminosis:
-dermatitis
-ulcers of mucosa
spasms, paresis
-hypolipidemia,
-liver steatosis
➢ Source: yeast, liver, eggs, fish, bread
➢ Daily req.: 10-15 mg

8. Chemical and physiological name, coenzymes, biological

role of vitamin B5.
Answer:
➢ Chem name: nicotinic acid, nicotinamide, niacin
➢ Phys name: antipellagric
➢ Coenzymes: NAD and NADP
➢ Take part in:
-glycolisis
-gluconeogenesis
-PPC
-FA synthesis and oxidation
-AA deamination
-Krebs cycle (3 enzymes)
-ETC -nucleic acids formation
-FA synthesis
-cholesterol synthesis

9. Manifestations of hypovitaminosis, nature sources and

day requirement of vitamin B5.
Answer:
 ➢ Hypovitaminosis – disease pellagra(3D-
dermatitis,diarrhea, dementia)
Causes:
-malabsorption
-alcoholism
-protein starvation
-in persons who eat a lot of corn (lack of tryptophan from
which В5 can be synthesized by bacteria)
➢ Source: liver, meat, fish, eggs, yeast, black bread
➢ Daily req.: 14-25 mg

10.Chemical and physiological name, coenzymes, biological

role of vitamin B6.
Answer:
Chem name: pyridoxine
Phys name: antidermatitic
Coenzymes: pyridoxal phosphate(PLP) and pyridoamine
monophosphate(PMP)
PLP and PMP – coenzymes of enzymes of AA metabolism:
-amino transferases
-decarboxylases
-participate in oxidation of amines
-synthesis of GABA
11.Manifestations of hypovitaminosis, nature sources and
dayly requirement of vitamin B6.
Answer:
➢ Hypovitaminosis
-in the using of antagonists (isoniazid, penicyllamine, L-DOPA,
estrogens)
-in malabsorbtion, alcoholism
-increased requirement in pregnancy
➢ Sources: beans, fish, bread, cereals, nuts, eggs, legumes,
meat
➢ Daily req.: 2-3 mg

12.Chemical and physiological name, coenzymes, biological

role of vitamin B10.
Answer:
Chem name: folic acid
Phys name: antianemic
Coenzymes: tetrahydrofolic acid(THFA)
➢ Biological role of THFA: transfers of methyl groups in the
synthesis of:
- aminoacids;
- purine nucleotides;
- creatin;
- methionin.

13.Manifestations of hypovitaminosis, nature sources and

day requirement of vitamin B10.
Answer:
In deficiency – disorders of the NA and protein synthesis,
inhibition of growth and cell division.
➢ Symptoms:
-hyperchromic megaloblastic anemia
-leucopenia
-thrombocytopenia
-glossitis,
conjuctivitis,
gastritis (disorders of epithelium proliferation)
-growth inhibition
-impairment of the wound healing
-immunodeficiency
➢ Food: bean, green leafy vegetables, lemons,
mushrooms, meat, liver
➢ Daily req: 200-500 mg
14.Chemical and physiological name, coenzymes, biological
role of vitamin B12.
Answer:
Chem name: cyanocobalamin
Phys name: antianemic
Coenzymes: - 5-deoxyadenosyl-cobalamin
- меthylcobalamin
Biological role:
-tightly connected to folic acid
-synthesis of methionine from homocysteine
-synthesis of creatin, cholin
-synthesis of phospholipids
-synthesis of purine and pyrimidine bases, nucleic acids.

15.Manifestations of hypovitaminosis, nature sources and

day requirement of vitamin B12.
Answer:
Symptoms: -hyperchromic megaloblastic anemia (malignant,
pernicious, Addison-Birmer disease)
-fatty dystrophy of nervous cells, neurological disorders
-cardiovascular disorders (accumulation of homocystein)
Sources: eggs, meat, poultry, shellfish, milk and milk products
Daily req: 2-5 mg
16.Chemical name, biological role of vitamin H.
Answer:
Chem name: biotin
Phys name: antiseborheic
Coenzyme of carboxylase, serves as transporter of carboxylic
group
-Pyruvate carboxylase
– gluconeogenesis
-Acetyl-СоА carboxylase,
propionyl-СоА carboxylase
– lipid metabolism

17.Chemical name, structure, active forms and properties of

vitamins C. Biological role of vitamins C.
Answer:
➢ Chem name: ascorbic acid
➢ Phys name: antiscorbutic
➢ Active form: L- ascorbic acid
➢ Properties: has oxidation-reduction properties
➢ Biological role:
➢ -reduces sulhydryl groups of proteins, enzymes
➢ -formation of serotonin
➢ -synthesis of norepinephrine
 ➢ -synthesis of steroid hormones
➢ -formation of carnitin
➢ -synthesis of collagen (hydroxyprolin)
➢ -formation of THFA
➢ -decomposition of hemoglobin -Fe3+ → Fe2+ -
absorption in the intestine
➢ -promote immunity defence

18.Manifestations of vitamins C hypovitaminoses. Scurvy.

Answer:
Hypovitaminosis - scurvy:
-Dot hemorrhages (petechiae)
- loose of teeth, gums swell and bleed easily (collagen deficit)
-anemia (lack of THFA)
-pain in heart, swelling of legs, weakness, fatigue
-loss of weight
Daily requirement: 75- 100 mg

19.Chemical name, properties, biological role of vitamin P.

Answer:
Chem name: bioflavonoids
Phys name: factor of permeability
Structure – compounds having phenolic structure
Biological role:
–synergist of vitamin C
-protects vitamin C against oxidation
-hydroxylation of proline and lysine
-inhibit hyaluronidase
-prevent oxidation of epinephrine
-antioxidants

20.Clinical symptoms of vitamin P hypovitaminosis.

Answer:
Hypovitaminosis:
-petechiae
-symptoms of scurvy

21.Nature sources and day requirement of vitamins P.

Answer:
Daily requirement: 50-75 mg
Food: pepper, citrus, black currant, rowan, buckwheat, fruits

22.The differences of fat soluble vitamins from water

soluble vitamins.
Answer:
23.Chemical and physiological name, structure and
provitamins of vitamin A.
Answer:
Chem name: Retinol
Phys name: Antixeropthalmic
Structure: Biochemically, there are 3 vitamin A structures
that differ on the basis of the functional group on C-1:
hydroxyl (retinol), carboxyl (retinoic acid), and aldehyde
(retinal).
Active forms •Retinol •Retinal •Retinoic acid
24.Biological role of vitamins A. The role of vitamin A in the
visual cycle.
Answer:
➢ Modulator of biomembranes
➢ changes the permeability
➢ synthesis of membranes components
➢ Growth vitamin
➢ stimulates the synthesis of proteins (especially in
cartilages)
➢ stimulates the synthesis of purine and pyrimidine
nucleotides
➢ Participates in oxidation-reduction reactions
➢ Regulates the synthesis of keratin (prevents the
conversion of cylindrical epithelium into horny)
➢ Promotes the spermatogenesis and placenta
development
➢ Stimulates the synthesis of antibodies and phagocytosis
(antiinfectious)
➢ Regulates the hormonal status
➢ prevents the oxidation of vitamin C
➢ inhibits the synthesis of thyroxin Maintains the
antioxidant potential of different tissues
VISUAL CYCLE
➢ Vit A is respo. For visual cycle.
➢ Rod-cells are adapted to sensing low light intensities;
they are the cells involved in night vision.
➢ Cone cells, which sense colors, are adapted for high light
intensities.
➢ Retinal rod cells contain many membrane vesicles that
serve as light receptors.
➢ About one-half of the protein in the membrane consists
of the light-absorbing protein rhodopsin (visual purple).
➢ Rhodopsin - chromoprotein that is present in the outer
segment of the rods.
➢ Rhodopsin consists of a protein, opsin, and tightly
bound 11-cis-retinal, the aldehyde of vitamin A.
➢ When rhodopsin is exposed to light, the 11-cis-retinal
undergoes transformation into all-trans-retinal, which
causes a substantial change in the configuration of the
retinal molecule.
➢ Enzyme – retinal isomerase .
➢ In order for rhodopsin to be regenerated from opsin and
all-trans-retinal, the latter must undergo isomerization
back to 11-cis-retinal.
➢ This appears to occur in a sequence of enzymatic
reactions: - all-trans-retinal + NADH + Н+ → all-trans-
retinol + NAD+ ( enzyme - alcohol dehydrogenase (or
called retinene reductase) using NADH;
➢ all-trans-retinol → 11-cis-retinol (enzyme - retinol-
isomerase - 11-cis-retinol + NAD+ → 11-cis-retinal +
NADH + H+ enzyme - alcohol dehydrogenase (called
retinene reductase)
➢ The 11-cis-retinal so formed now recombines with opsin
to yield rhodopsin, thus completing the visual cycle
25.Clinical symptoms of vitamin A hypovitaminosis and
hypervitaminosis.
Answer:
Vit A hypovitaminosis causes night blindness, Anemia, incr.
susceptibility to infection and cancer, follicular
hyperkeratosis, xeropthalamia, keratomalacia, bronchitis,
pneumonia, cystitis, cysts in salivary glands, pyelonephritis.
Vit A hypervitaminosis
➢ Excessive vit A leads to toxicity
➢ Symptoms: dermatitis, enlargement of liver, skeletal
decalcificatiom, loss of weight, tenderness of long
bones, loss of hair, joint pains, irritability, etc

26.Nature sources and day requirement of vitamins A.

Answer:
Daily requirement: 2-3 mg
Sources: eggs, meat and dairy products, green leafy veg,
intensely coloured fruits and vegetables.

27.Chemical and physiological name, structure and

provitamins of vitamin D.
Answer:
Chem name: cholecalciferol
Phy name: antirickets
Vit D is 7-dehydro-cholesterol
•Vitamin D2 – ergocalciferol (plant)
•Vitamin D3 – cholecalciferol (animals)

28.The mechanism of formation of vitamin D active forms.

Answer:
Vit D2 and D3 are not biologically active but are converted in
to active forms by
TWO HYDROXYLATION reactions:
A. Hydroxylation of Vit D3 at the 25-position by a specific
hydroxylase in the liver results in formation of 25-OH D3
or 25-hydroxycholecalciferol which is major storage
form of Vit D and predominant form of Vit D in
circulation.
 B. 23 OH D3 is further hydroxylated at one position by
specific 1-hydroxylase in kidney resulting in formation
of 1-25 dihydroxy cholecalciferol.
1-25 dihydroxycholecalciferol is the most potent VitD
metabolite and its formation in kidney is regulated by
PTH.

29.Biological role of vitamins D. Clinical symptoms of

vitamin D hypovitaminosis. Rickets.
Answer:
Functions of vitamin D
➢ regulates the Ca and P levels in the blood
➢ promotes absorption of Ca and P in the intestine
➢ promotes reabsorption of Ca in the kidneys
➢ high levels of serum Ca and P increase the rate of bone
mineralization
➢ promote bone resorption (at low Ca in blood)
➢ promotes phagocytosis
➢ immunomodulatory activity
➢ induces differentiation of immune cells
➢ Activates reabsorption of amino acids, especially prolin
➢ Activates the monosaccharides phosphorylation
(glycogen synthesis)
➢ Promotes ATP formation
Hypovitaminosis D
Rickets softening of bones in children potentially leading to
fractures and deformity
 Causes:
➢ vitamin D deficiency
➢ lack of calcium in the diet
➢ severe diarrhea and vomiting
➢ fat malabsorption
➢ alcoholism
➢ severe liver and kidney diseases
Signs and symptoms of rickets
➢ Bone pain or tenderness
➢ Dental problems
➢ Muscle weakness
➢ Fractures (easily broken bones)
➢ Skeletal deformity
➢ Bowed legs (genu varum)
➢ Knock-knees (genu valgum) or "windswept knees"
➢ Cranial, spinal, and pelvic deformities
➢ Hypocalcemia
➢ Tetany (uncontrolled muscle spasms)
➢ Craniotabes (soft skull)
➢ Widening of wrist (due to metaphysial cartilage
hyperplasia)

30.Nature sources and day requirement of vitamin D and

hypervitaminosis.
Answer:
Daily req: 12-25 mg
Sources: Sunlight, cheese,butter, margarine, fortified milk,
fish and fortified cereals
Hypervitaminosis
•Increase of Ca and P in blood
•Demineralization of bones
•Calcification of inner organs
•Renal stones

31.Chemical and physiological name, biological role of

vitamin E.
Answer:
Chem name: tocopherols and tocotrienols
Most active – alpha-tocopherol
Phys name: anti-sterile
Biological role:
➢ Most potent antioxidant
➢ Active scavenger of free oxygen and nitrogen radicals
➢ Protects vit. A from oxidation
➢ Prevents oxidation of Se
➢ Stabilizes the cell membranes
➢ Increases the resistance of membranes to oxidation and
toxic effects
➢ Improves cellular respiration stabilizing ubiquinone
➢ Prevents oxidation of LDL
➢ Reduces risk of atherosclerosis
 ➢ Regulates transcription
➢ Maintains normal immune function
➢ Inhibits cholesterol biosynthesis

32.Nature sources and day requirement of vitamin E and

hypervitaminosis.
Answer:
Sources: corn, nuts, green, leafy veg., vegetable oils, wheat
germ, olives.
Daily req.: 20-50 mg
Hypervitaminosis
➢ Vit E, being fat soluble if exceeds than normal amount
can accumulate inside our body and gives certain side
effects.
➢ Nause
➢ Gastric distress
➢ Headache
➢ Fatigue
➢ Diarrhea
➢ Abdominal cramps
➢ Easy bruising and bleeding

33.Chemical and physiological name, biological role of

vitamin K.
Answer:
Chem name: Quinone derivatives
Phys name: Antihemorrhagic
K1, phyloquinone (in green vegetables)
K2, menaquinone (is synthesized by intestinal bacteria)
Biological funct:
➢ Stimulate synthesis of coagulation factors in liver
➢ Stimulate the synthesis of albumins, pepsin, trypsin,
lipase, amilase
➢ Inhibits free radical oxidation
➢ Increases the resistance of capillaries
➢ Increases the peristalsis in intestine

34.Chemical and physiological name, biological role of

vitamin F.
Answer:
10-15 mg
Chem name: polyunsaturated fatty acids
Phys name: Antisclerotic
Major representatives:
Linoleic acid
Linolenic acid
Arachidonic acid
Biological role:
 ➢ Participate in the organism growth and development
➢ Components of phospholipids (cell membranes)
➢ Regeneration of skin epithelium
➢ Synthesis of prostaglandins
➢ Decrease cholesterol level
➢ Increase the organism resistance

35.The blood functions, their characteristic.

Answer:
1. Gas transport – blood carries oxygen from lung to the
tissues and carbon dioxide in reverse direction.
2. Transport of nutritional substances for all cells (glucose,
amino acids, fatty acids, vitamins, ketone bodies,
microelements etc.). Blood carries final products of
metabolism (urea, uric acid, bilirubin, creatinin etc.) from
tissues to kidney, where from they excreted with urine.
3. Regulation of different processes. Blood creates and
carries local hormones (hormonoids) to the target organs.
4. Thermoregulation – heat change between tissues and
blood.
5. Osmotic function – maintenance of the osmotic pressure
in blood vessels.
6. Protective function – blood has antibodies and leucocytes,
which perform phagocytosis.
7. Detoxification – blood enzymes can neutralize (split)
different toxic substances.
8. Coagulation, the response to a broken blood vessel, the
conversion of blood from a liquid to a semisolid gel to stop
bleeding

36.Biochemistry of blood cells. Function of leucocytes.

Answer:

➢ Two types of blood cells can be distinguished - white

and red blood cells.
➢ White blood cells are called leucocytes. Their quantity in
adult is 5000-9000/l.
 ➢ Red blood cells are called erythrocytes. Their quantity in
peripheral blood is 4,2 – 6 millions/L.
➢ Besides that, there are also thrombocytes or platelets in
blood.
➢ Leucocytes are divided into two groups: Granulocytes
and agranulocytes.
➢ Granulocytes consist of neutrophils, eosinophils and
basophils.
➢ Agranulocytes consist of monocytes and lymphocytes.

37.Respiratory function of erythrocytes.

Answer:
➢ Erythrocytes consists of a conjugated protein which
functions as respiratory pigment.
 ➢ carries oxygen from the lungs to the body's tissues and
returns carbon dioxide from the tissues back to the
lungs.

38.Structure and biological role of hemoglobin.Types of

hemoglobin.
Answer:
Hemoglobin - is the protein molecule in red blood cells that
carries oxygen from the lungs to the body's tissues and
returns carbon dioxide from the tissues back to the lungs.
Quantity and chemical structure of hemoglobin
➢ In man – 130-160 g/L;
➢ In woman – 120-140 g/L.
➢ Hemoglobin consists of protein part - "globin", that
contain 4 polypeptide chains.
➢ 2 Alfa-chain consist 146 aminoacid residues;
➢ 2 Beta-chain - 142 aminoacid residues.
➢ Nonprotein part of hemoglobin called – heme.
Types of hemoglobin
➢ HbA1 (α2β2 ) - main type of hemoglobin in blood of
adult people (96 %) is the form containing two alpha and
two beta chains.
➢ HbA2 (α2δ2 ) about 2 % of adult hemoglobin
➢ HbF (α2 γ2 ) - 2-3 % of fetal hemoglobin HbF has a
higher affinity to O2.
➢ After birth Hb F replaced by Hb A.
39.Pathological hemoglobin’s.
Answer:
Carboxyhemoglobin- HbCO
➢ The binding of oxygen is affected by molecules such as
carbon monoxide (CO). CO completes with oxygen at the
heme binding site.
➢ Hemoglobin binding affinity for CO is 200 times greater
than its affinity for oxygen.
➢ When hemoglobin combines with CO, it forms a very
bright red compound called carboxyhemoglobin.
Methemoglobin
➢ When ferrous(fe+2) iron is oxidised to ferric(fe+3),
metHb is formed
➢ Methemoglobin cannot bind oxygen. In human blood a
trace amount of methemoglobin is normally produced
spontaneously, but when present in excess the blood
becomes abnormally dark bluish brown.
➢ The NADH-dependent enzyme methemoglobin
reductase is responsible for converting methemoglobin
back to hemoglobin.
Causes of methemoglobin formation:
1. Various pharmaceutical compounds
2. Environmental agents :
Aromatic
amines
Arsine
 Chlorobenzene
Chromates
Nitrates
Nitrites
3. Inherited disorders

40.Derivatives of hemoglobin, conditions of their

appearance.
Answer:
1. Physiological hemoglobin derivatives
Oxyhemoglobin - it is used for transport of O2 in the body
(HbO2).
HbCO2 carbhemoglobin
2. Pathological derivatives of hemoglobin
Carboxyhemoglobin-HbCO and
Met-Hb Fe3+
41.The contents of total proteins in blood plasma. The main
proteins of blood plasma.
Answer:
One liter of plasma contain 65-85 gram of proteins.
Concentration of:
• albumins is 35-50 g/L;
• globulins is alpha-1-globulins – 1-4 g/L,
• alpha-2-globulins – 4-8 g/L,
 • beta-globulins – 6-12 g/L,
• gamma-globulins – 8-16 g/L;
• fibrinogen – 2-4 g/L.
➢ Plasma which are not contain fibrinogen called serum (it
is necessary for understanding the immunology, therapy
etc.)

42.Albumins: content in blood plasma, physical and

chemical properties. Functions of albumins.
Answer:
➢ albumins is 35-50 g/L;
➢ Makes up approximately 60% of the total plasma
protein.
➢ About 40% of albumin is present in the plasma, and the
other 60% is present in the extracellular space.
➢ Half life of albumin is about 20 days.
➢ Mature human albumin consists of one polypeptide
chain of 585 amino acids and contains 17 disulfide
bonds
➢ It has an ellipsoidal shape, which means that it does not
increase the viscosity of the plasma as much as an
elongated molecule such as fibrinogen does.
➢ Has an isoelectric pH of 4.7
FUNCTIONS:
➢ Colloidal osmotic Pressure - albumin is responsible for
75–80% of the osmotic pressure of human plasma due
to its low molecular weight and large concentration
 ➢ It plays a predominant role in maintaining blood volume
and body fluid distribution.
➢ Hypoalbuminemia leads to retention of fluid in the
tissue spaces (Edema)
➢ Transport function - albumin has an ability to bind
various ligands, thus acts as a transporter for various
molecules.
➢ These include-  free fatty acids (FFA), calcium,
certain steroid hormones, bilirubin, copper
➢ A variety of drugs, including sulfonamides, penicillin G,
dicoumarol, phenytoin and aspirin, are also bound to
albumin
➢ Nutritive Function Albumin serves as a source of amino
acids for tissue protein synthesis to a limited extent,
particularly in nutritional deprivation of amino acids.
➢ Buffering Function - Among the plasma proteins,
albumin has the maximum buffering capacity due to its
high concentration and the presence of large number of
histidine residues, which contribute maximally towards
maintenance of acid base balance.
➢ Viscosity- Exerts low viscosity

43.Globulins: content in blood plasma, physical and

chemical properties. Functions of globulins.
Answer:
• globulins is alpha-1-globulins – 1-4 g/L,
• alpha-2-globulins – 4-8 g/L,
• beta-globulins – 6-12 g/L,
 • gamma-globulins – 8-16 g/L;
They are glycoproteins
Based on electrophoretic mobility , they are sub classified in
to α1 and α2 globulins
Examples-
α1 antitrypsin
α1 -fetoprotein (AFP)

44.Fibrinogen: content in blood plasma, functions.

Answer:
• fibrinogen – 2-4 g/L.
• Also called clotting factor1
• Constitutes 4-6% of total protein
• Imparts maximum viscosity to blood
• Synthesized in liver
• Made up of 6 polypeptide chains
• Negative charge contributes to its solubility in
plasma and prevents aggregation due to
 electrostatic repulsions between the fibrinogen
molecules.
Fibrinogen helps in blood clotting

45.Causes and consequences of hyperproteinemia and

hypoproteinemia., types.
Answer:
Hyperproteinemia - increase of the total contents of proteins
in blood plasma.
There are two types of hyperproteinemia - absolute and
relative.
Absolute hyperproteinemia – accumulation of the proteins
in blood. It occurs in infection and inflammatory diseases
(hyperproduction of immunoglobulins), rheumatic diseases
(hyperproduction of C-reactive protein), some malignant
tumors (myeloma) and others.
Relative hyperproteinemia – the increase of the protein
concentration but not the absolute amount of proteins. It
occurs when organism loses water (diarrhea, vomiting,
fever, intensive physical activity etc.).
Hypoproteinemia - decrease of the total contents of proteins
in blood plasma. This state occurs in old people as well as
in pathological states accompanying with the oppressing of
protein synthesis (liver diseases) and activation of
decomposition of tissue proteins (starvation, hard
 infectious diseases, state after hard trauma and
operations, cancer).
Hypoproteinemia (hypoalbuminemia) also occurs in kidney
diseases, when the increased excretion of proteins via the
urine takes place

46.Transport forms of blood lipids: - chylomicrons.

Answer:
➢ are the largest lipoproteins (180 to 500 nm in diameter)
• are synthesized in the intestinal cells
• contain 85 % of TGs (it is the main transport form
of dietary TGs).
• apoprotein B-48 (apo B-48) is the main protein
component
• deliver TGs from the intestine (via lymph and
blood) to tissues (muscle for energy, adipose for
storage).
• bind to membrane-bound lipoprotein lipase (at
adipose tissue and muscle), where the
triacylglycerols are again degraded into free fatty
acids and monoacylglycerol for transport into the
tissue
• are present in blood only after feeding

47.Transport forms of blood lipids:-low density lipoproteins;

Answer:
48.Residual nitrogen, components, content in blood.
Answer:
Residual nitrogen – nonprotein nitrogen, that is nitrogen of
organic and inorganic compounds that remain in blood
after protein sedimentation.
Organic and inorganic compounds of residual nitrogen are as
follows:
- urea (50 % of the residual nitrogen),
- amino acids (25 %),
- creatine and creatinine (7,5 %),
- salts of ammonia - indicane (0,5 %),
- other compounds (about 13 %).
- Urea is formed in liver during the degradation of amino
acids, pyrimidine nucleotides and other nitrogen
containing compounds.
- Amino acids are formed as result of protein decomposition
or owing to the conversion of fatty acids or carbohydrates
to amino acids. The pool of amino acids in blood is also
supported by the process of their absorption in intestine.
- Creatine is produced in kidneys and liver from amino acids
glycine and arginine, creatinine is formed in muscles as
result of creatine phosphate splitting. In result of ammonia
neutralization the ammonia salts can be formed.
- Indicane is the product of indol neutralization in the liver.
The content of residual nitrogen in blood is 0,2 – 0,4 g/l.

49.General description of theimmune system; cellular and

biochemical components.
Answer:
➢ The purpose of the immune system is to keep infectious
microorganisms, such as certain bacteria, viruses, and
fungi, out of the body, and to destroy any infectious
microorganisms that do invade the body.
➢ The immune system is made up of a complex and vital
network of cells and organs that protect the body from
infection.
50.Immunoglobulins: structure, biological functions
mechanisms of immunoglobulins action.
Answer:
➢ Antibodies are known as immunoglobulins
• Globular glycoproteins
• The heavy and light chains are polypeptides
• The chains are held together by disulphide bridges
• Each ab has 2 identical ag binding sites – variable
regions.
• The order of amino acids in the variable region
determines the shape of the binding site
How Abs work
• Some act as labels to identify antigens for
phagocytes
• Some work as antitoxins i.e. they block toxins for
e.g. those causing diphtheria and tetanus
• Some attach to bacterial flagella making them less
active and easier for phagocytes to engulf
• Some cause agglutination (clumping together) of
bacteria making them less likely to spread
51.Biochemical components of the system of complement;
classical and alternative
Answer: These are covered by nine central components of
the cascade (C1 to C9), multiple activation products (such
as C3a and C3b), regulators and inhibitors (e.g. Factor H
and C4BP), proteases and newly assembled enzymes (e.g.
C4b2a and Factor B), or effector molecule receptors (such
as C3aR and C5aR)
52.mechanisms of it activating.
53.Liver’s functions.
Answer:
1.Liver is a main organ which is responsible of nutritional
substances in our organism (for example, glucose,
triacylglicerides and ketone bodies).
2.All types of metabolism (protein, lipid, carbohydrate,
vitamins, mineral) take part in liver.
3. Hepatocytes synthesizes blood lipoproteins, lowweight
bioactive substances (creatin, 25- cholecalciferol, heme),
cholesterol.
4. Synthesis of urea (final product of nitrogen metabolism)
also takes place in the liver.Liver functions
5. Liver synthesizes bile acids and excrete a bile into intestinal
tract. This process play a very important role in lipids
digestion and excretion of cholesterol.
6. Liver play detoxification role, inactivates endogenic and
exogenic substances (ammonia, metabolic waste, drugs,
alcohol and chemicals, some hormones, different toxins).
7. Liver is a depo for iron and some another metals.
8. Liver synthesize blood plasma proteins and non-essential
amino acids.
9. Liver synthesizes purine and pyrimidine nucleotides,
creatine, nicotinic acid, choline, carnitine, polyamines.
10. Liver stores glucose in the form of glycogen which is
converted back to glucose again when needed for energy.
11. Liver stores the vitamins A, D, E, B10, B12 and synthesizes
blood clotting factors

54.Role of liver in regulation of vitamin metabolism and

water-salts balance.
Answer:
Regulation of vitamin metabolism:
• Formation of active form of vitamin D
• Formation of vitamin A from carotins
• Depo of cyanocobalamine and folic acid
• Depo of vitamin E
 • Phosphorilation of vitamins B, formation of
coenzyme forms.
Regulation of water-mineral balance:
Liver acts as a storage site for iron, copper

55.The decomposition of hemoglobin in tissues, bile

pigments formation.
Answer:
• After a life span of about 120 days the erythrocytes
die.
• The dead erythrocytes are taken up by the
phagocytes of the
• reticuloendothelial system of the body (spleen,
bone marrow, liver).
• The Hb molecule is broken down into 3 parts:
• The protein part (globin) of Hb is utilized partly in
to aminoacids or to other body proteins.
• The iron is stored in the reticuloendothelial cells
and is used for the synthesis of Hb and other iron
containing substances of the body.
• The porphyrin part of heme converted in to bile
pigments.
• Heme in the presence of the enzyme, heme
oxygenase, loses one molecule of CO and one atom
of iron in Fe3+ form producing biliverdin.
 • In this reaction, the porphyrin ring is cleaved by
oxidation of the alpha methenyl bridge between
pyrrole rings.
• The enzyme needs NADPH+H+ and O2.
56.Direct and indirect bilirubin, true and false urobilin.
Answer:
Direct and indirect bilirubin
• Bilirubin formed in reticuloendothelial cells then is
associated with plasma albumin to protect cells
from the toxic effects.
• Bilirubin associated with plasma proteins cannot
pass into the glomerular filtrate in the kidney; thus
it does not appear in urine.
• This bilirubin is called - indirect bilirubin or free
bilirubin or unconjugated bilirubin.
True and False Urobilin
• A small part of urobilinogen is reabsorbed by the
mucous of intestine and via the vessels of vena
porta system enter to liver. In hepatocytes
urobilinogen is used for formation of pyrol
compounds which are excreted with bile. This
urobilinogen in urine is called urobilin, or true
urobilin.
• Another bile pigment that can be reabsorbed in the
intestine is stercobilinogen. From the blood
stercobilinogen pass via the kidneys into the urine
where it is oxidized to stercobilin. Another name of
urine stercobilin is false urobilin.
57.The mechanism of jaundices formation, their
biochemical characteristics.
Answer:
• Jaundice or icterus is the orange-yellow
discoloration of body tissues which is best seen in
the skin and conjunctivae;
• it is caused by the presence of excess of 35 mcmol/l
bilirubin in the blood plasma and tissue fluids.
• Jaundice can be classified as
o pre-hepatic,
o hepatic and
o post-hepatic

58.Kinds of jaundice, short description.

Answer:
59.Prehepatic jaundice. Causes, biochemical characteristic.
Answer:
Jaundice due to the excessive breakdown of red blood cells.
• Causes:
• sickle cell anemia
• Malaria
• Thalassemia
 • Autoimmune disorderds
• Massive hemorrhage

60.Hepatic jaundice. Causes, biochemical characteristic.

Answer:
occurs due to the liver disease and inability of liver to
metabolize and remove bilirubin from the biliary system
Causes:
• •Liver cirrhosis,
• •Liver cancer,
• •Viral hepatitis,
• •Gilbert’s syndrome,
• toxins or drugs, etc.
Hepatic jaundice is characterized by
 • 1. Increased levels of conjugated and unconjugated
bilirubin in blood serum.
• 2. Dark coloured of urine due to the excessive
excretion of urobilinogen.
• 3. Pale, clay coloured stools due to the absence of
stercobilinogen.
• 4. Increased activities of alanine and aspartate
transaminases.

61.Posthepatic jaundice. Causes, biochemical characteristic.

Answer:
is caused by obstruction of bile flow from the liver
Causes:
• •carcinoma of the bile duct or gall bladder;
• •presence of gallstones in the biliary system;
• •infection by parasites;
• •pancreatitis, etc
characterized by:
1. Increased concentration mainly of conjugated bilirubin in
blood serum.
2. Dark beer coloured urine due to elevated excretion of
conjugated bilirubin and clay coloured feces due to
absence of stercobilinogen
62.Types of reactions of bio transformations of xenobiotics
in a liver.
Answer:
Xenobiotics are toxic compounds that are foreign to the
body.
The principal classes of xenobiotics:
Exogenic xenobiotics - medical relevance are drugs, chemical
cancerogens, (insecticides, herbicides, pesticides, food
additions, cosmetics, domestic chemical substances).
Endogenic xenobiotics - some internal substances also have
toxic properties (for example, bilirubin, free ammonia,
bioactive amines, products of amino acids decay in the
intestine). Moreover, all hormones and mediatores must
be inactivated.
Biological transformation of xenobiotics.
• hydrolysis,
• reduction,
• oxidation.
These reactions introduce production of new functional
groups (—OH, —NH2 , —SH, or — COOH) and usually
result in a little increase of hydrophylic properties in
xenobiotics.
63.Reactions of microsomal oxidation;
Answer:
Microsomal oxidation system consist - cytochrom P450 and
flavin enzyme P450 reductase
Catalyzes monooxigenation of oxygen atom into substrate;
another oxygen atom is reduced to water
Electrons are transferred from NADPH to cytochrome P450
through flavoprotein NADPH-cytochrome P450 reductase..

64.Reactions of conjugation in the hepatocytes: biochemical

mechanisms, functions.
Answer:
Phase II – conjugation includes:
glucuronation,
sulfation,
acetylation,
methylation,
conjugation with glutathione,
conjugation with aminoacids (glycin, taurin, glutamic acid)
Phase II results in the marked increase of hydrophylic
properties of xenobiotic.
Glucuronation, the combining of glucuronic acid with toxins,
requires the enzyme UDP-glucuronyl transferase (UDPGT).
Many of the commonly prescribed drugs are detoxified
through this pathway. It also helps to detoxify aspirin,
menthol, vanillin (synthetic vanilla), food additives such as
benzoates, some hormones and bilirubin
Sulfation is the conjugation of toxins with sulfur-containing
compounds. The sulfation system is important for
detoxifying several drugs, food additives, and, especially,
product decay of proteins, toxins from intestinal bacteria
and the environment. Sulfation is also used to detoxify
some normal body chemicals and is the main pathway for
the elimination of steroid and thyroid hormones.
Glutathione is also an important antioxidant. This
combination of detoxification and free radical protection,
results in glutathione being one of the most important
anticarcinogens and antioxidants in our cells, which means
that a deficiency is cause of serious liver dysfunction and
damage.
65.Kidney functions in organism:
Answer:
➢ Excretion of the end products (metabolites, drugs,
toxins);
➢ Urine formation;
➢ Homeostatic function: -
• maintenance of acidic-base balance;
• maintenance of water-salt balance;
• maintenance of osmotic pressure;
➢ Hormonal activity .
• rennin synthesis (blood pressure regulation)
• erythropoietin (erythrocytes formation),
• 1,25-dihydroxycholecalcipherol (vitamin D3 )
➢ Metabolism of proteins, lipids, carbohydrates, energetic
metabolism

66.Mechanism of urine formation – filtration.

Answer:
Structures responsible for the urine formation:
➢ glomeruli,
➢ proximal canaliculi,
➢ distal canaliculi.
Mechanism of urine formation:
➢ filtration
 ➢ reabsorption
➢ secretion
Filtration
➢ Takes place in glomeruli.
➢ Substances with molecular mass below 40,000 Da pass
through the membrane of glomerulus into capsula.
➢ About 120 mL/min or 180 L/day of blood is filtrated.
➢ Filtration – passive process. In result of filtration formed
primary urine (urine without proteins -180 L/day)
➢ Filtration is caused by:
➢ -hydrostatic pressure of blood in capillaries of glomeruli
(70 mm Hg)
➢ -oncotic pressure of blood plasma proteins (30 mm Hg)
➢ -hydrostatic pressure of ultrafiltrate in capsule (20 mm
Hg)
➢ 70 mm Hg-(30 mm Hg+20 mm Hg)=20 mm Hg
➢ Hydrostatic pressure in glomeruli is determined by the
ratio between diameter of ascendant and descendant
arteriole

67.Mechanism of reabsorbtion, secretion.

Answer:
Reabsorption
➢ Takes place in proximal and distal canaliculi.
➢ Reabsorption - is the process by which the nephron
removes water and solutes from the tubular fluid and
returns them to the circulating blood.
 ➢ Reabsorption:
active
passive.
➢ Lipophilic substances - passive.
➢ Na/K АТP-аse is very active
➢ 3 groups of reabsorption substances :
1. Substances, that actively reabsorbed
2. Substances, that small reabsorbed
3. Substances, that not reabsorbed
➢ Active reabsorbtion - glucose and proteins (100%),
amino acids (93%), water – 96%, NaCl (70%) etc.
➢ Small reabsorbed - urea and uric acid.
➢ Not reabsorbed - creatinin, manitol - (sugar alcohol) and
inulin - (polimer of fructose).
Secretion
➢ Transport of substances from blood into filtrate.
➢ Takes place in proximal and distal canaliculi.
➢ Secretion:
active
passive.
➢ Passive secretion depends on the pH.
➢ What is secreted?
•Ions of K, аmmonia, H+
•drugs
•Xenobiotics .
•After secretion primary urine convert into secondary
urine
68.Notion about clearance. Regulation of urine formation.
Answer:
➢ Clearance of any substance is expressed in ml of blood
plasma that is purified from this substance for 1 min
while passing through the kidneys.
➢ About 180 L of primary urine is formed for 1 day, about
125 mL of primary urine for 1 min.
➢ Glucose is reabsorbed completely; clearance = 0 Inulin is
not reabsorbed absolutely; clearance = 125 mL/min
➢ If clearance is more than 125 mL/min the substance is
secreted actively.
➢ Clearance = (C urine/C plasma) * V
Regulation of urine formation
➢ Corticoid adrenal male sex hormone and thyroxine
inhibit the reabsorption of water, thereby increasing
urine output.
➢ Parathyroid hormone and antidiuretic hormone
(vasopressin), reduce the secretion of urine by
increasing the absorbability of water.
➢ Vasopressin regulated by the nervous system depending
on the amount of liquid in the blood with the help of
osmoregulation reflex. The excess hormone is excreted
in the urine.
➢ Adrenaline in small quantities narrows the excretory
vessels of the kidney, raising the pressure in the
nephrons. And in large doses can lead to the cessation
of urine due to the narrowing of the arteries leading.
69.Physical and chemical characteristics and components of
urine:
Answer:

➢ Normal urine is transparent or clear; becomes cloudy

upon standing.
➢ Cloudy urine may be evidence of phosphates, urates,
mucus, bacteria, epithelial cells, or leukocytes.
➢ Density – 1,003-1,035 g/mL
➢ Increased density – organic or inorganic substances
available (diabetes mellitus)
➢ Decreased density – diabetes insipidus
➢ Isostenuria – continuously low density in oliguria (kidney
failure)
 ➢ pH – 5.5-6.8
➢ Acidic – meat food, diabetes mellitus, starvation, fever
➢ Alkaline – plant food, cystitis, pyelitis

70.Pathological components of urine, which appear due to

different metabolic disorders in organism:-urobilinuria;-
creatinuria;-indicanuria;- phenylketonuria.
Answer:
71.The kinds of proteinuria. Renal proteinuria: causes and
characteristic.
Answer:
 renal is
same as tubular.

72.Indexes of renal functions disorders: proteinuria,

hematuria.
Answer:
Hematuria, or haematuria,

is the
presence of red blood cells (erythrocytes) in the urine. It
may be idiopathic and/or benign, or it can be a sign that
there is a kidney stone or a tumor in the urinary tract
(kidneys, ureters, urinary bladder, prostate, and urethra),
ranging from trivial to lethal. If white blood cells are found
in addition to red blood cells, then it is a signal of urinary
tract infection.
Causes The most common causes of hematuria[2] are:
• Urinary tract infection with viruses,[2] other sexually
transmitted diseases (particularly in women)[2] or some
bacterial species including strains of EPEC and
Staphylococcus saprophyticus
• Bladder stones
• Kidney stones or ureter stones
• Benign prostatic hyperplasia, in older men, especially those
over 50

73.Indexes of renal functions disorders: glucosuria, pyuria,

creatinuria
Answer:
74.Structural and chemical peculiarities of muscles.
Answer:
75.Structure and functions of sarcoplasma proteins
(Myogene, Myoglobine,
Answer:

Myogen fraction contain (enzymes of glycolysis and

respiratory chain);
myogen - proteins extracted from skeletal muscle with cold
water, largely the enzymes promoting glycolysis; from the
residue, alkaline 0.6 mol L-1 KCl extracts actin and myosin
as actomyosin, with myosin further separable into two
meromyosins by proteinase treatment.
76.Myoalbumine.
Answer:

Human albumin is a small globular protein (molecular

weight: 66.5 kDa), consisting of a single chain of 585 amino
acids organized in three repeated homolog domains (sites
I, II, and III). Each domain comprises two separate sub-
domains (A and B) 5

77.Muscles stroma proteins.

Answer:
•collagen
•keratin
•elastin are constituents of connective tissue of vessel walls,
nerves, sarcolema.

78.Mechanism of muscle’s contraction.

Answer:
79.Mechanism of muscle’s relaxation. Role of calcium and
ATP.
Answer:
Importance of Calcium Ions. Ca2+ ions play an
important role in muscle contraction by creating
interactions between the proteins, myosin and actin.
The Ca2+ ions bind to the C component of the actin
filament, which exposes the binding site for the myosin
head to bind to in order to stimulate a muscle contraction.

80.Energetic providing of muscle’s work.

Answer:
81.Red and white muscles.
Answer:
Red fibers
➢ •Lot of myoglobin and mitochondria
➢ •Oxidative phosphorylation is active
➢ •Are contracted slowly, for a long time, no tiredness for
long time
➢ •Aerobic oxidation
White fibers
➢ •Little hemoglobin and mitochondria
➢ •More glycogen
➢ •Glycolisis is specific
➢ •Are contracted fast, fast tiredness
➢ •Anaerobic oxidation
82.Peculiarities of metabolism in cardiac muscle.
Answer:
83.General description of connective tissue.
Answer:
Connective tissue - is a kind of biological tissue that supports,
connects, or separates different types of tissues and
organs of the body.
Connective tissue present in all organs (50 % of body weight)
➢ •Skin;
➢ •Adipose tissue;
➢ •Bones;
➢ •Teeth;
➢ •Fascia;
➢ •Cartilages;
➢ •Stroma of parenchymal inner organs;
 ➢ •Walls of vessels.
Functions of connective tissue:
- Storage of energy
- Protection of organs
- Provision of structural framework for the body
- Connection of body tissues
- Connection of epithelial tissues to muscle tissue.

84.Structure and functions of collagen.

Answer:
Consists of three polypeptide chains having the left spiral
shape
Three left coiled chains are again coiled together to form the
right spiral bunch
1 chain contains about
➢ 1000 amino acids
➢ 33 % - glycine
➢ 21 % – proline and oxiproline
➢ 11 %– alanine
➢ 35 % – all other amino acids
Oxiproline and oxilysine are specific only for connective
tissue
Collagen – complex protein, glycoprotein
Carbohydrates (monosaccharide galactose and disaccharide
galactosylglucose) bind by glycosidic bonds to the residues
of oxilysine of polipeptide chain.
There are 12 types of collagens (differ from each other by
the:
- primary structure;
- types of chains;
- contents of carbohydrates;
- localization in organs and tissues.
85.Structure and functions of proteoglycans
Answer: