CHAPTER 1 - LIPIDS is a lipid that exists as a solid at room

LIPIDS - Lipids are a heterogeneous group of temperature.

compounds, including fats, oils, steroids, waxes, b. Unsaturated fats:

and related compounds, that are MORE are lipids that exist in liquid form at room

RELEVANT for their physical properties than temperature.

their chemical properties. TRANSFAT - is a lipid that has undergone a

- PROPERTIES: process called hydrogenation.

(1) relatively insoluble in water and (2) soluble 2 TYPES OF UNSATURATED FATS

in nonpolar solvents such as ether and 1. Monounsaturated

chloroform 2. Polyunsaturated

- FUNCTION: - Omega-3 fatty acids:

Energy STORAGE form. Important food may help prevent and even treat heart disease

ingredient due to its high energy value, and stroke

insulating effect, shaping and contouring the PHOSPHOLIPIDS:

body These lipids are made up of two fatty acids and a

- CLINICAL SIGNIFICANCE: phosphate group, component of cell membranes

obesity, atherosclerosis, fatty liver STRUCTURE:

3 TYPES LIPIDS: Glycerol + 2 fatty acids + phosphate group

1. Triglycerides: STEROLS:

fats and oils includes cholesterol, bile acids, sex hormones,

2. Phospholipids: adrenocorticotropic hormones and vitamin D.

lecithin CLASSIFICATION OF LIPIDS

3. Sterols: 1. Simple lipids:

cholesterol Esters of fatty acids with various alcohols

FATS: a. Fat:

Fats are the largest class of lipids and are also Esters of fatty acids with glycerol. Oil is a fat in

known as triacylglycerols, triglycerides and a liquid state

glycerolipids b. Waxes:

- STRUCTURE: Esters of fatty acids with monohydric alcohols

Glycerol + 3 fatty acids of higher molecular weight

2. Complex lipids:

- TYPE: Esters of fatty acids containing groups other than

a. Saturated: alcohols and fatty acids

a. Phospholipid:
Lipids, in addition to fatty acids and alcohols, 2. Classification of fatty acids based on
also have phosphoric acid residues hydrophobic chain length
b. Glycolipids: - Short chain - has 2 to 6 carbon atoms
Lipids containing fatty acids, sphingosine and - Medium chain - has 8 to 14 carbon atoms
carbohydrates - Long chain - with 16-18 carbon atoms
c. Other complex lipids: - Very long chain fatty acids - with 20 or more
Lipids such as sulfolipids and aminolipids carbon atoms
3. Lipid precursors and derivatives: BIOLOGICAL IMPORTANCE OF FATTY
fatty acids, glycerol, steroids, other alcohols, ACIDS
fatty aldehydes, ketone bodies 1. constituent of dietary fat eat
Fatty acids: 2. required for the formation of membrane lipids
fatty carboxylic acids, they are mainly exists as such as phospholipids and glycolipids
an ester in natural fats and oils but exists in an 3. required for the esterification of cholesterol to
unesterified form as free fatty acids, a transport form cholesteryl esters
form found in plasma 4. act as fuel molecules
CLASSIFICATION OF FATTY ACIDS
1. According to the nature of the anaerobic chain
water
a. Saturated - Saturated fatty acids can be
considered to be based on acetic acid
b. Unsaturated:
i. Monounsaturated:
contains double bond
ii. Polyunsaturated:
acids, containing two or more double bonds.
MEANING:
liquid at room temperature.
c. Branching:
Phytanic acid found in butter
d. Replace:
Cerebronic Acid - Fatty Acid OH
e. Period:
Chalmoogric acid and hydnocarpic acid
CHAPTER 2 PROTEIN 3. Vasopressin (antidiuretic hormone, ADH):

PROTEIN: ADH is also a nonapeptide produced by the

nitrogen-containing organic macromolecules and posterior pituitary gland. It stimulates the

the most abundant, widely distributed in animals kidneys to retain water and thus increases blood

and plants. pressure.

Structural Function: CLASSIFICATION OF AMINO ACIDS

Certain proteins are primarily responsible for the BASED ON THEIR METABOLIC FATE

structure and strength of the body. 1. Glycogen amino acids:

Dynamic functions: These amino acids can act as precursors to the

Dynamic functions of proteins are more diverse formation of glucose or glycogen. For example.

in nature. They include proteins that act as alanine, aspartate, glycine, methionine, etc.

enzymes, hormones, clotting factors, 2. Ketogenic amino acids:

immunoglobulins, membrane receptors, storage Fats can be synthesized from these amino acids.

proteins, in addition to controlling genetics, Two amino acids, leucine and lysine, have only

muscle contraction, respiration, etc. ketogenic properties.

STRUCTURE: 3. Glycogen and ketogenic amino acids:

Each amino acid has two functional groups; an The four amino acids isoleucine, phenylalanine,

amino group –NH2, a carboxylic acid group – tryptophan, tyrosine are precursors for the

COOH and a hydrogen atom –H, each attached synthesis of glucose as well as fat.

to the carbon next to the –COOH group. PROTEIN CLASSIFICATION

FUNCTIONS OF ACIDS A. Functional classification of proteins

1. Serotonin is formed from tryptophan B. Classification of proteins based on their

2. Tyrosine forms hormones such as thyroid chemical nature and solubility

hormone C. Nutritional classification of proteins

INTRODUCTION TO PEPTIDES A. Classification of functions of proteins

1. Glutathione: Depending on the function they perform,

(reduced) performs specialized functions in red proteins are classified into:

blood cells 1. Structural proteins:

- participates in detoxification processes. Hair and nail keratin, bone collagen.

2. Oxytocin: 2. Enzyme or catalytic protein:

It is a hormone secreted by the posterior Hexokinase, pepsin.

pituitary gland and contains 9 amino acids 3. Transport proteins:

(nonapeptide). Oxytocin causes the uterus to Hemoglobin, serum albumin.

contract. 4. Endocrine proteins:

Insulin, growth hormone.
5. Contractile proteins:
Actin, myosin.
6. Reserve protein:
Ovalalbumin, glutelin.
7. Genetic Proteins:
Nucleoproteins.
8. Defense proteins:
Snake venom, Immunoglobulin.
9. Receptor protein:
for hormones and viruses.
B. Classification of proteins based on chemical
nature and solubility Based on the composition,
structure, shape and solubility properties of
amino acids.
1. Simple Proteins:
They consist only of amino acid residues.
2. Conjugated Proteins:
In addition to amino acids, these proteins also
contain a non-protein segment called a
prosthetic or conjugated group.
3. Derived protein:
This is a denatured or decomposed product of
simple proteins and conjugated proteins.
C. Nutritional classification of proteins
The nutritional value of proteins is determined
by the composition of essential amino acids.
first. Complete Protein:
These proteins contain ten essential amino acids
in the proportions required by the human body
to promote good growth. For example. egg
albumin, milk casein.
4. Partially incomplete proteins:
These proteins are partially missing one or more
essential amino acids and can support moderate
growth. For example. wheat and rice proteins
(Lys, Thr limited). 3. Incomplete Proteins:
These proteins are completely devoid of one or
more essential amino acids. Therefore; they do
not promote growth at all, e.g. gelatin (Trp
deficient), zein (Trp, Lys deficient).
PROPERTIES OF PROTEIN
1. Solubility:
Protein forms a colloidal solution instead of
forming a true solution in water. This is due to
the enormous size of protein molecules.
2. Molecular Weight:
Proteins vary in molecular weight, which, in
turn, depends on the number of amino acid
residues. Each amino acid contributes an
average molecular weight of about 110 Daltons.
• Insulin-5,700; Myoglobin-17,000;
Hemoglobin- 64,450; Serum albumin-69,000.
3. Shape:
It can be spherical (insulin), oval (albumin),
fibrous or elongated (fibrinogen).
4. Isoelectric pH:
The nature of amino acids (especially their
ionized groups) determines the pI of
CHAPTER 3 MACRO and MICRO Alopecia (hair loss)
NUTRIENTS Diarrhea
1. IRON Excessive body odor
2.ZINC TOXICITY
3.COPPER Nausea and vomiting Abdominal pain
4.IODINE COPPER
5.MANGANESE Enzyme cofactor in iron metabolism, melanin
6. FLUORIDE synthesis, electron transport
7.MOLYBDENUM DEFICIENCY
8.COBALT White hair, Gray hair, Brittle hair, Varicose
9.SELENIUM veins
10. CHROMIUM Ptosis, Reduced glucose tolerance Menke’s
MINERALS Kinky hair syndrome
 Large class of ESSENTIAL Menke’s Kinky Hair Syndrome
MICRONUTRIENTS
1.MACROMINERALS – required in large
quantities, 100 mg/day. IODINE
2.MICROMINERALS – required in small •Combines with T4 or tyrosine to produce
quantities, less than 100 mg/day. thyroxine.
MICRO •Promotes metabolism
IRON DEFICIENCY= GOITER
•Helps carry oxygen to body tissues including GRAVE’S DISEASE
muscle DEFICIENCY Symptoms:
IRON DEFICIENCY ANEMIA ◦ Insomnia
KOILONYCHIA ◦ Heat intolerance
Liver disease ◦ Excessive sweating
Arrhythmias ◦ Exopthalmos
ZINC ◦ Rapid pulse
•Important in function of many enzymes ◦ Irritability
•Wound healing MANGANESE
DEFICIENCY •it activates numerous enzyme systems including
Infertility those involved with glucose metabolism, energy
Failure of wounds and ulcers to heal production
Poor growth
•Responsible for the development of fragile ear Cancer
bones and joint cartilage Irregular heart beat
Toxicity- PSYCHIATRIC DISORDERS
RESEMBLING SCHIZOPHRENIA MACRO
POTASSIUM 1.CALCIUM
•Vital for muscle contractions and nerve 2.PHOSPHORUS
transmission 3.MAGNESIUM
•Important for heart and kidney function 4. SULFUR
•Helps regulate fluid balance and blood pressure CALCIUM
DEFICIENCY •Helps build strong bones and teeth
Muscular weakness •Involved in muscle contractions and nerve
mental apathy function
Cardiac failure •CALCIUM
DEFICIENCY>>OSTEOMALACIA
CALCIUM TOXICITY
Muscle and abdominal pain
CHROMIUM Calcium kidney stones
•Works with insulin for proper glucose • PHOSPHORUS
metabolism •Works with calcium to build and maintain
DEFICIENCY bones and teeth
Low blood sugar •Helps convert food to energy
Diabetes •Regulates blood pH
Hyperinsulemnia Phosphorus Deficiency
Hyperactivity Aggravates osteoporosis, arthritis, high blood
Infertility and pressure, loose teeth, etc.
decreased sperm count loss of appetite
SELENIUM Weakness
•Involved in fat metabolism Pain
•Cooperates with vitamin E Phosphorus Toxicity
•Acts as an antioxidant Lowers blood calcium which may lead to
DEFICIENCY tetany and convulsions
Age spots MAGNESIUM
Muscular weakness •production and transfer of energy for protein
Infertility synthesis
•for contractility of muscle and excitability of
nerves
•cofactor in myriads of enzyme systems
DEFICIENCY
-Asthma, Anorexia, Menstrual migraines,
Growth failure
- ECG changes, Neuromuscular problems,
Tetany (Convulsions)
TOXICITY
Inhibited bone calcification
Low blood pressure
Drowsiness
Nausea
Slurred speech
Unsteadiness

SULFUR
•Attached to proteins to maintain:
1.Hemoglobin
2.Hormones (Insulin, adrenal cortical hormones)
3.Enzymes
4.Antibodies
DEFICIENCY
degenerative types of arthritis involving
degeneration of cartilage, ligaments, tendons
Systemic Lupus Erythematosis
Sickle cell anemia
various "collagen diseases."
SECTION 4 MINERALS • POOR HAIR HEALTH
Vitamins and minerals are = • POOR SKIN HEALTH
MICRONUTRIENTS
CLASSIFICATION OF VITAMINS VITAMIN D: important compounds in this
1. Water soluble: Vitamin B1-B7, B9, B12, group are:
Vitamin C – cannot be stored, extracted from the - vitamin d3 – cholecalciferol
body - vitamin d2 – ergocalciferol
2. Fat soluble: Vitamins A, D, E, K – can be Synthesis of vitamin D in the skin is the major
stored in fat cells, when there is excess it can be natural source of the vitamin
absorbed in the intestinal tract FUNCTION: essential for the proper
utilization of calcium and phosphorus to produce
Vitamin A = Vitamin A refers to three normal, healthy bones.
biologically active vitamers NORMAL VALUES: 600 IU
- Retinol DEF: Rickets (caused by lack of sunlight, but
- Retinal also from insufficient calcium), retarded growth
- Retinoic acid
refers to several provitamin carotenoids - (most VITAMIN E - is the collective name for a
notably beta-carotene) group of fat-soluble compounds with distinctive
FUNCTION: antioxidant activities, TOCOPHEROL IS THE
- Functions in eyesight(retinal) and bone ONLY FORM THAT IS RECOGNIZED TO
formation MEET HUMAN REQUIREMENTS, BEAUTY
- It is important in the ration of pregnant VITAMIN
females
- Mechanism of vision Sources are nuts, seeds
- Rodopsin synthesis Vit E = thickens hair, muscle strength
- Antioxidant 15 mg = NORMAL VALUE
- Reproduction Most of the functions of Vit. E are related to its
NORMAL AMOUNT – 600-900 antioxidant properties
 300mg = hypervitaminosis TOXICITY – Hypervitaminosis
DEF: Retardation in young, night blindness, DEFICIENCY – Ataxia, retinopathy, hair loss
Reproductive disorders VITAMIN K - PHYLLOQUINONE IS THE
DISEASES: MAIN DIETARY FORM OF VITAMIN K
POOR IMMUNITY NORMAL VALUE – 75 mcg
• ANEMIA TOXICITY – liver damage
DEFICIENCY – extreme bleeding - Skin Rashes
SYMPTOMS OF DEF – nosebleeds, bleeding - Slower Release Of Insulin
gums, blood in urine - Lower Vitamin C And Vitamin B6 Level
VITAMIN B3 - High Blood Sugar Level
FUNCTIONS – release of energy, synthesis of VITAMIN C
fats and protein, act of coenzyme, vasodilation - Acidic nature
Normal Range – 0.50-0.85ug/Ml - Strong reducing agent
Pellagra – Dermatitis, Diarrhea, Dementia, - Cannot be synthesized by humans
Death - Mostly present in retina, thymus and adrenal gland

Toxicity: FUNCTIONS:

- Tachycardia, IRON AND HEM METABOLISM

Act as cofactor
- Itching
Bone formation
- Gout
Formation of norepinephrine
- Abdominal Pain
Toxicity Occurs When Niacin Intake Is More
MATURATION OF ERYTHROCYTES –
Than 1000mg/Day
STEROID SYNTHESIS
B5 Pantothenic Acid - Immunological Function
FUNCTIONS – related to CoA - Reduces Cataract Formation
Involved in most of the metabolism - Antioxidant Function
DEFICIENCY – very rare DEFICIENCY:
- Usually malnourished individuals Occurs Due To:
- Anorexia nervosa - Dietary Deficiency-Anorexia Nervosa
- Malabsorption - Impaired Absorption Deficiency Leads To Scurvy
Normal Range: 1.6 To 2.7 Mcmol/L - Normal Serum Level- 0.3-0.6mg/Dl

- No Toxicity Arises Due To Excessive Intake Of

Pantothenic Acid

Rda Adult: 10mg/Day Children: 7mg/Day

Vitamin B7

Normal Blood Biotin Level 400-1200ng/L

Deficiency - Consuming Raw Egg

Toxicity Is Rare

- Can Occur During Prolong Overdose Of Biotin

Clinical Symptoms Includes
CHAPTER 5 NUCLEIC ACIDS - It is caused by the imminent action of acids or

a. Simple proteins (histones): thymus, enzymes

pancreas and nucleoproteins (nucleo-tissues) - Not soluble in water.

- Produces large amounts of lysine and arginine. b) Derivative proteins - proteases

- Combined with nucleic acids in cells - Intermediate product of protein digestion

b) Scleroproteins: - Soluble in water.

- connective tissues and hard tissues. - Does not coagulate when exposed to heat.

- Fibrous proteins do not dissolve in all - Precipitated with saturated ammonium sulfate

solvents. - Resistant to digestion - The result of partial digestion of proteins with

a) Conjugated proteins - nucleoproteins: pepsin or trypsin. c. Derivative proteins -

cytoplasm of cells, nucleus of chromosomes and peptones

ribosomes, viruses and bacteriophages - Intermediate product of protein digestion

- It contains nucleic acids, nitrogen and - Same properties as proteases, except they

phosphorus. cannot be salted.

- It occurs in chromosomes and in all living - Lower molecular weight than proteases. d.

forms as a combination of protein with either Derivative proteins - peptides

DNA or RNA. - Intermediate product of protein digestion

b) Conjugated proteins - mucoprotein - Two or more amino acids joined by a peptide

- Saliva (Mucin) and egg white (Ovomucoid). - bond.

Proteins combined with amino sugars, sugar - Hydrolyzed into individual amino acids.

acids and sulfates. STRUCTURE OF PROTEINS:

c. Conjugated proteins - glycoproteins 1. Primary structure: The amino acid

- Bones (Oseomucoid), tendons (Tendomucoid) sequence of a polypeptide chain is called the

and cartilage (Chondromucoid). primary structure.

- Contains more than 4% hexamine, - Amino acids are connected to each other by

mucoproteins; if less than 4%, then peptide bonds.

glycoproteins 2. Secondary structure of proteins:

d. Conjugated proteins - Peptide chains can be helical or zig-zig.

- phosphoproteins - This coiling of peptide chains is called the

e. - Milk (casein) and egg yolk (ovo vitelline). secondary structure of proteins.

- Phosphoric acid joined the protein with an 3. The Tertiary Structure Of Proteins:

ester bond. a) Derivative proteins - proteins Twisting or folding of polypeptide chains

- Edestan (elastin) and myosin (myosin). represents tertiary structure of proteins

4. The Quaternary Structure Of Proteins:
- Quaternary means four. It is the arrangement
of multiple folded protein or coiling protein
molecules in a multi-subunit complex. - Various
bonding interactions, including hydrogen bonds,
salt bridges and disulfide bonds, keep the
different chains in specific geometries.

Properties of proteins
- Found in all living organisms.
- Involved in processes such as digestion, cell
structure, catalysis, movement, energy
processing, etc.
- Complex molecules
The importance of proteins
- formation of protoplasm
- Nucleoproteins are complex proteins and act
as carriers of hereditary materials from one
generation to another. - Enzymes are biological
catalysts and they are also proteins
- Hemoglobin is a protein. It acts as an oxygen
carrier.
- Tanning of hides is actually precipitation of
proteins by tannic acid.
- Gelatin is obtained by heating bones, skins and
tendons in water. It is used in bakery goods
- Casein is another protein used in manufacture
of buttons and buckles.
- Proteins obtained from soya bean are used for
manufacture of plastics.