Introductory One written answers

1) Mention 4 sultar containing GAGS and the

function of two of them
• Sulfate containing glycosaminoglycans: e.g. chondroitin
sulphate, keratan sulphate, dermatan sulphate, heparin and
heparan sulphate.
• Heparin : is an important anticoagulant (prevents thrombus
formation), it acts by binding with factor IX and XI. Also, it
produces activation of antithrombin. It binds specifically to
lipoprotein lipase enzyme and increases its release form the
capillary wall to the plasma. This enzyme helps in removal
and clearance of blood lipids.
• Keratan sulfate proteoglycan is important for transparency of
the cornea.
• Heparan sulfate plays an important role in cell membrane
receptors and cell-cell interactions.
2) Explain GAGS has shock absorbing
property

The negatively charged carboxylate and sulfate groups on the

proteoglycan bind positively charged ions and form hydrogen
bonds with trapped water molecules, thereby creating a hydrated
gel. This gel is compressible when a GAG solution is compressed,
water is squeezed out and GAGs occupy a smaller volume. When
the compression is released, their molecules regain their original
hydrated size. This gives GAGs solutions the shock absorbing
properties.
 3) Enumerate types of glycerophospholipids

1. Phosphatidic acid (Diacylglycerolphosphate).

2. Lecithin (Phosphatidylcholine).

3. Cephalin (Phosphatidylethanolamine).

4. Phosphatidylserine.

5. Phosphatidylinositol (Lipositol).

6. Phosphatidylglycerol.

4) Enumerate Types of eicosanolds

They are classified into 2 main groups:
A- Cyclic compounds (prostanoids):
1- Prostaglandins (PG)
2- Prostacyclins
3- Thromboxanes (TX)
B- Acyclic compounds:
1- Leukotrienes (LT). (PGI)
2- Lipoxins (LX)
5) Enumerate 4 importance of phospholipids

1) Phospholipids are amphipathic molecules that carry non-glacial

groups of fatty acid side chains and polar groups of glycerol,
phosphate, serine, ethanolamine, choline and inositol. They form
micelles in water.

2) They are good emulsifying factors, important for digestion and

absorption of dietary fats.
3) They are good hydrotropic substances; they prevent deposition
of cholesterol as cholesterol stones (biliary calculi).

4) They are important constituents of plasma lipoproteins.

5) They are important constituents of the lipid bilayer in cell

membranes

6) They provide arachidonic acid for the synthesis of eicosanoids.

7) They are essential for blood clotting, as they provide the platelet
activating factor (PAF), which is a plasmalogen that contains
choline, palmityl alcohol at position 1 and acetic acid at position 2.
8) Lung surfactant is formed mainly of dipalmitoyl-lecithin, the
lack of which is responsible for respiratory distress syndrome in
premature infants.

9) They play as mediators for hormonal activity:

6) Explain phospholipids are important in lung

protection

As Lung surfactant is formed mainly of dipalmitoyl-lecithin, the

lack of which is responsible for respiratory distress syndrome in
premature infants.

7) Explain chaperones deficiency may lead to

disease.

chaperones use different mechanisms to promote efficient protein

folding and prevent aggregation. Decline in chaperones allows the
expression of several protein-aggregation diseases, including
Alzheimer's disease and Parkinson's disease
 8) Collagen has very firm structure ..explain

1-Each turn contains 3 amino acid residues (makes a tight helix)

normal proteins 3.6 a.a. per turn.

2- The presence of glycine with its short side chain makes the
polypeptide chains very close to each other.

3-The 3 left handed coiled peptide chains form a right handed

super helix.

4-The high content of hydroxyproline forms hydrogen bonds

between chains.

5-The formation of covalent cross linkages between the ε amino

group of lysine and the hydroxylysine of adjacent polypeptide
chains are responsible for tensile properties of collagen

6- The specific arrangement into fibril and fibers.

7- The staggered array gives marked flexibility to collagen.

9) Explain osteogenesis imperfecta develops

due to collagen disorder

The most common mutation is the replacement of glycine residues

by amino acids with bulky side chains which prevents the
formation of the required triple helical conformation.

10) Mention main types of thalassemia

1- α-Thalassemias: These are defects in which the synthesis of α -
globin chains is decreased or absent:
a- Silent carrier of α-thalassemia: One of the four genes is
defective.
 b- α-Thalassemia trait: Two α-globin genes are defective.
c- α-Thalassemia major: Three α-globin genes are defective.
d- Homozygous α-thalassemia: The four α-globin genes are
defective
2- β-Thalassemias: -In these disorders, synthesis of β-globin
chains is decreased or absent, whereas α-globin chain synthesis
is normal. individuals with β-globin gene defects have either β-
thalassemia trait (β-thalassemia minor) if they have only one
defective β-globin gene, or β-thalassemia major if both genes
are defective.
11) Mention mechanism of sickle cell anemia
Sickle cell disease is a genetic disorder of the RBCs caused by a
single nucleotide alteration in the β globin gene in which the polar
glutamate at position six has been replaced with a nonpolar valine.
The nonpolar amino acid generates a hydrophobic “sticky patch”
on the surface of the β subunit of both oxyHbS and deoxyHbS.
Both HbA and HbS contain a complementary sticky receptors on
their surfaces that is exposed only in the deoxygenated state Thus,
at low PO2, deoxyHbS can polymerize to form long, insoluble
fibers producing rigid, mis-shaped erythrocytes. Such sickled cells
frequently block the flow of blood in the narrow capillaries.
(infarction) The spleen removes sickle cells at a faster rate than
normal cells, leading to hemolytic anemia.
12) Mention different isozymes of lactate
dehydrogenase and their significance

Isozymes of LDH Type of subunits

1- I1 (H4 or HHHH)
 2- I2 (H3M1 or HHHM)
3- I3 (H2M2 or HHMM)
4- I4 (H1M3 or HMMM)
5- I5 (M4 or MMMM)

clinical importance: Isozyme 1 is mainly of cardiac origin and its level

in plasma increases in cases of myocardial infarction. Isozyme 5
increases in plasma in cases of liver diseases (hepatic origin) or
muscle diseases (muscular origin).

13) Explain creatine kinase is Used in diagnosis

of myocardial Infarction

Creatine kinase is a dimer formed of two subunits termed M or B.

It has three isozymes one of them is CK2 (or CK-MB) present
mainly in cardiac muscles and its plasma level increases in
myocardial infarction.

14) Mention definition and two examples of

uncouplers

These are substances which uncouple respiratory chain oxidation from

phosphorylation the process of oxidation will proceed without
phosphorylation (no ATP production), and thus the energy of the reaction
will be dissipated or lost in the form of heat. These substances increase
the permeability of the inner mitochondrial membrane to protons.
Examples: : 2, 4-dinitrophenol and dinitrocresol.

15) Mention examples of high energy bond

High energy phosphate bonds e.g. ATP and creatine phosphate

High energy sulfur bonds, eg. Acyl CoA, S-adenosylmethionine.
 16) Mention examples of low energy bond
1- Phosphate ester bonds, e.g. G-6-P.\
2- Glycosidic bonds in carbohydrates.
3- Peptide bonds in proteins.
4- Carboxyl ester bonds in triacylglycerol.
17) Mention two characters of DNA Primary
Structure. ( write any 2 points )
• The nucleotides that form DNA primary structure are mainly
four: dAMP, dGMP, dCMP and dTMP.
• In each strand, the nucleotides are linked together by
phosphodiester bonds between the 5`-hydroxyl of one
nucleotide and 3`-hydroxyl of the next nucleotide.
• The alternating sugar phosphate units form the backbone of
each DNA strand (5`-P-S-P-S-3`).
• The nitrogenous bases, which are linked to the pentoses, are
projecting to the inside of the two strands of DNA at right
angle.
• Each polynucleotide strand has two terminals. One end has a
free phosphate group attached to 5`-hydroxyl group of the
terminal pentose and the other end has a free 3`- hydroxyl
group.
• The order of nucleotides in any DNA strand is always written in
the 5` to 3` direction, which is the direction of synthesis.
18) Mention two characters of DNA Secondary
Structure. ( write any 2 points )
1- Two antiparallel strands form a right-handed helix The two
strands of DNA are paired to each other and coil around a
common axis to form a right-handed helix. The two strands run
 antiparallel, that is to say, one runs in the 5` to 3` direction and
the other in the 3` to 5` direction.
2- Complementary base pairing The two strands are held together
by the complementary base pairing through specific hydrogen
bonds. Adenine pairs with thymine through two hydrogen bonds,
and guanine pairs with cytosine through three hydrogen bonds.
3- Base stacking :The base pairs inside the helix are stacked above
each other by Van der Waals forces and hydrophobic interactions.
4- Spiral staircase The double helix of DNA appears much like
spiral staircase, in which there are 10.4 base pairs or steps for
each complete turn of the helix. Each complete turn is 3.4 nm
long.
5- Dimensions The B-form of DNA is 2 nm wide. From outside of
the helix, two grooves are apparent, a major groove (2.2 nm) and
a minor groove (1.2 nm).