HAMZA COLLEGE OF HEALTH SCIENCES,

SARGODHA

Subject: Biochemistry

PHARMACY TECHNICIANS 1ST YEAR

IMPORTANT QUESTIONS & MCQS

Chapter # 1
Carbohydrates
1. Define Carbohydrates. Classify them with suitable examples.
Definition
“Carbohydrates are polyhydroxy aldehydes or ketones or their complex substances which on
hydrolysis give polyhydroxy aldehydes or ketones” The carbohydrates are the organic compounds.
Carbohydrates also called sugar”

The carbohydrates are classified into Four groups.

1. Monosaccharide: having one sugar molecule and cannot hydrolyze to smaller units 2.
Disaccharide: Having two sugar molecule and give two monosaccharide on hydrolysis.
3. Oligosaccharides: Having 3-10 sugar molecules. on hydrolysis yield 3-10
monosaccharides.
4. Polysaccharide: having more than ten sugar molecules and give disaccharide on hydrolysis
and on further hydrolysis the monosaccharide is met.
2. Define polysaccharides. Classify them and write their importance.
Definition
Having more than ten sugar molecules and give disaccharides on hydrolysis and on further
hydrolysis the monosaccharide is met. Many saccharides (Sugar Molecules) join to form poly
saccharides.
They are tasteless and not optically active
There are two types of polysaccharides.
1) Homopolysaccharides: The polysaccharides which yield one type of monosaccharide
on hydrolysis is called homopolysaccharides’ Starch, Glycogen
2) Heteropolysaccharides: The polysaccharides which yield different types of
monosaccharide on hydrolysis called heteropolysaccharides.e. g Mucilage’s, Hemi
cellulose

Examples of polysaccharides:
Cellulose: Most abundant on earth present in cell wall of plants. Starch: It
is stored food material in plants, in corns, grains etc. Glycogen: It mainly
occurs in animal muscles and liver.
Starch: It occurs in grains, seeds and tubers Types: (i) Amylose (ii) Amylopection

3. Carbohydrates are major source of energy Justify this statement.

1) The simple sugars are absorbed directly by the small intestine into blood stream.
2) But the disaccharide and polysaccharide do not absorbed in blood directly first convert
into monosaccharide.
3) This bond breaking also provides energy.
4) Then the monosaccharides are absorbed by blood.
5) When the molecules are oxidized so produced a high amount of energy “ this is the
principle used by carbohydrates to give energy.
C6H12O6 + O2 ––––––→ CO2 + H2O + E( ATP)
4. Describe the structure and functions of Monosaccharides.
“Having one sugar molecule and cannot hydrolyze to smaller units”
Characteristics
• They are sweet in taste.
• It cannot further hydrolysis.
• Generally they are water soluble.
• Two types of functional group: 1. Aldehyde group 2. Keto group
Classification of monosaccharide

Monosaccharide can be classified on the basis of functional group i) Aldose ii) Ketose

1) Aldose
i. Glucose: (C6H12O6)
 It is also called grape sugar. It is widely distributed in nature. It combines with other sugars
to form important disaccharides such as sucrose, maltose, and lactose. It is the main sugar
of human body. Normal blood glucose level of human in fasting 80_100mg% and in
random is 100__120mg%. Glucose is also called dextrose.
ii) Ribose: (5 Carbon Sugar) iii) Erythrose: ( 4 Carbon Sugar) iv) Glucoheptose: ( 7
Carbon Sugar)
2) Ketose
i. Fructose: (C6H12O6)
The most common source of fructose is sucrose.
It is sweetest of all the sugars. Pure honey
contains fructose. It is present in appreciable
amount in seminal fluid and act as source of
energy for spermatozoa ii) Erythrulose: iii)
Ribulose:
iv) Sedoheptulose

Chapter # 2
Lipids
1. Define Lipids. Classify them with suitable examples and state their functions.
Definition
The lipids are organic substances occurring in plant and animal tissues belong to a very
heterogeneous group of compounds related to fatty acids.
These are classified as,
I. Simple Lipids (Fatty Acids + Alcohol)
II. Compound Lipids (Fatty Acids +Alcohol + Add. Group) III.
Derived Lipids (Hydrolysis of Simple or Compounds Lipids)

FUNCTIONS OF LIPIDS
1. Energy source: They are good source of energy.
2. Carrier of fat – soluble vitamin: Lipid in food also acts as a carrier of fat-soluble vitamins
and nutritionally essential fatty acids.
3. Dietary Lipids: The dietary lipids decrease gastric motility and have a high satiety value.
 4. Stability: Body fat gives anatomical stability to organs like kidney. When a person loses
weight rapidly, his kidney is liable to become floating kidneys.
5. Good reservoir: Fats are good reservoir in the body. Adipose tissue is best suited for this
purpose due to its very little water content.

2. Define Simple Lipids and Explain them with suitable examples.

Definition
Esters of fatty acids with various alcohols.
1. FATS AND OILS
These are esters of fatty acids with glycerol. (Trihydroxy alcohol). They are known as
triglyceride or triacylglycerol or fat. A fat in liquid state called oil Fats & oils are lighter
than water and have specific gravity of about 0.8
Glycerol+3Carboxylic acid -------→Triglycerides+3CO2+3H2O

2. WAXES
Definition These are esters of fatty acids with long chain monohydric alcohols.
RCOOH + ROH ―→ RCOOR + H2O
Waxes are widespread in nature as secretion of certain insects as protective coating of skin, e.g.
honey bee wax, fur of animals, certain animal oil & whale largely composed of waxes .

3. Classify Fatty Acids in various ways with suitable examples.

Definition:
Hydrolysis of fats is called fatty acid. Fatty acid contains long hydrocarbon chain bonded to –
COOH Group. They are aliphatic monocarboxylic acids.
Fatty acid may classify as,
Saturated fatty acids Unsaturated fatty acids

They do not contain double bond They contain one or more double bond in
their formula
Animal fat is usually saturated Plant fats are mostly unsaturated

Fats containing saturated fatty acids are Fats containing unsaturated fatty acids are
solids at room temperature liquid at room temperature
 Example Monounsaturated fatty acids
Butyric acid C3H7COOH i.e. Oleic acid C18H33COOH
Polyunsaturated fatty acids
i.e. Arachidonic acid C19H31COOH

4. Define Derived Lipids with suitable Examples.

Definition
These are esters of fatty acids containing groups in addition to an alcohol and fatty acids.
These are sub divided as follows:
1. Glycolipids also called Glycosphingolipids These contain sphinogosine, fatty acid and a
monosaccharide or an oligosaccharide unit.
2. Sulphosides These contain sphingosine, fatty acids, a sugar & a phosphate group.
3. Phospholipids These are lipids that contain an alcohol, fatty acid and phosphoric acid in
addition they frequently have N-containing bases & other substituents. 4. Lipoproteins These
are complex of lipid with proteins.

Chapter #3
Proteins 1.
Explain in detail the structural organization of proteins.
Proteins molecules have different several different level of structure.

Secondary structure Tertiary structure Quaternary structure

Primary structure
Linear sequence of Amino The next level of protein The overall three- Association of multiple
acids. Amino group is in one structure, secondary dimensional structure of a polypeptides, not found
side and left-hand side and structure, refers to local polypeptide is called its in all protein
carboxylic group on right hand folded structures that form tertiary structure. The
side. within a polypeptide due to tertiary structure is primarily
interactions between atoms due to interactions between
 the R groups of the amino
acids

Only Polypeptide linkage is Forms α helix and the β R group interactions that Aggregation of such
Present between Amino pleated sheet. contribute to tertiary polypeptides chain
Acids Hydrogen bond and structure include hydrogen form one functional
polypeptide bond is present bonding, ionic bonding or macromolecule
in Secondary structure. Disulphide bond
Length is vary according to Forms α helix and the β The final shape may be a globe Each poly peptide chain
proteins, length of chain pleated sheet. or an irregular shape is called subunit
depends upon type of proteins
Hormone Myocin Myoglobin. Collagen
Insulin Hemoglobin

2. Classify proteins in various ways and write their importance.

Proteins have been classified in several ways. The following classification is based upon
physicochemical properties of proteins. A protein may belong to one of the three types, I.
Simple proteins.
II. Compound or conjugated proteins
III. Derived proteins
1) SIMPLE PROTEINS
On hydrolysis, these proteins yield only amino acids or their derivatives.
These consist of the following types.
1. Albumins: These are water-soluble proteins and occur in both plant and animal kingdoms.
Examples are serum albumin, ovalbumin and lactalbumin m animals and legume in plants.
2. Globulins: These are insoluble in water but soluble in dilute salt solutions and are heat
coagulable to a variable extent. They are found in animals, e.g. lactoglobulin, myosin in muscle,
ovoglobulin, serum globulins and also in plants, e.g. legumin.
3. Globins These are rich in histidine but are not basic. They unite with heme to form hemoglobin.
Hemoglobin of different species differs only with respect to globin, but the heme part is the same
in all cases.
2) COMPOUND OR COUNJUGATED PROTIENS
In these molecules the protein is attached or conjugated to some non – protein groups which are
called prosthetic groups.
The following types of proteins belongs this group.
 i) Nucleoproteins. ii)
Phosphoprotien iii)
Lipoproteins
iv) Carbohydrate - containing proteins v)
Chromoproteins vi) Metalloproteins
2) DERIVED PROTEINS
This class of proteins includes substances which are derived from simple and conjugated
proteins. These proteins are sub divided into primary and secondary derived proteins.
1. Primary derived proteins: These are synonymous with denatured proteins. Denaturation takes
place when some or all of the cross -linkages which normally keep the molecular structure of
protein intact are split.
2. Secondary derived proteins: These substances are intermediate formed in the progressive
hydrolysis of protein molecule. The are of different sizes and different amino acid composition
and are roughly grouped according to their molecular size into a) Proteoses b) Peptones c)
Peptides d) Polypeptides e) Oligopeptide

Proteins have following some important role

1. Defense of body
Proteins are used against disease in higher animals. Antibodies and interferon are proteins in nature
in they defend the body from attack of bacteria and viruses (immunoglobulin). Protein is an
integral part of all viruses which are very important from a pathogenic point of view.
2. Contractility
Most proteins are involved in contractility e.g. dyne in cilia and flagella. Tubulin in spindle fibres.
Actin and myosin in muscles.
3. Exchange of gases
They execute their activities in the transport of O2 and CO2 by hemoglobin. Some act as hormones
e.g. insulin, growth hormones and parathyroid hormones etc. Muscles proteins have a role in
contraction of muscle fibres.e.g Antarctic fish contain antifreeze proteins which protect their blood
from freezing.
4. Blood clotting
They are involved in blood clotting through thrombin fibrinogen and other protein factors. The
proteins present in blood plasma act as a colloidal particles and exert and osmotic pressure of
25_30mmHg. The role of proteins in the plasma membranes where they act as transporting or carrier
molecules and receptors.

3. Classify amino acids in various ways with suitable examples.

Definition
Amino acids are the building blocks of proteins. They form protein by a biochemical bond called
Peptide bond or peptide linkage. Various number of amino acid joins to one another with peptide
bond to form “protein.
Amino acids typically are classified as standard or nonstandard Amino Acids.
1. Standard amino acids:
 The amino acids that are used to form proteins, only twenty amino acids take part in the
formation of all types of proteins. These twenty amino acids are called primary, standard or
normal amino acids.
Classification of Standard Amino Acids
This is based upon the type of side chain, i.e. R group present.
 Amino acids with non-polar aliphatic side chains
These include glycine Alanine, Valine. Leucine and Isoleucine.
 Amino acids with aromatic side chains
These include phenylalanine tyrosine and tryptophan and are said to be relatively polar.
 Side chain containing hydroxyl (-OH) group These include
serine and threonine.
 Amino acids with side chains containing sulfur (S) atom These
include cysteine and methionine.
 Amino acids with acidic side chains These include glutamic acid
and aspartic acid
 Amino acids with basic side chains These include lysine,
arginine and histidine.
 Amino acid
The only example of this type is proline.
1. Nonstandard protein amino acids:
These amino acids are not required to build proteins. These have a vital role as metabolic
intermediates. These are the derivative of amino acids and have role in metabolism. Alpha amino
butyric Acid, Citrulline, Ornithine, beta-alanine.

4. Explain the Watson and Crick model of DNA.

DNA contains the genetic information that gives rise to the chemical and physical properties
of living organisms The nucleotides in DNA are linked to each other in the same way as in
RNA

Watson and Crick in 1953 hypothesized that the DNA molecule is a double helix. The double
helix of DNA (nicknamed as coil of life) can be visualized as a spiral staircase wound around a
cylindrical axis. The bases are on the inside of the helix and the deoxyribose and phosphates on
the outside. The helix in most of the DNA is of right-handed type, i.e. the helix rises towards the
right. Double helix of DNA. A and B represent major and minor grooves respectively.
In DNA there are actually two antiparallel long molecules (each made up of a very long
polydeoxyribonucleotide chain) which are wound on each other. These two chains are joined to
each other throughout the whole length of the molecule through their respective nitrogenous bases.
In this joining together a purine only joins with pyrimidines. The helical structure repeats at
intervals of 3.4 nm and therefore there are. 10 base pairs in each completed helix. The helix is 2
nm in diameter. The molecule shows a minor groove and a major groove.

5. Explain the structure and functions of different type of RNAs.

RNA is a ribonucleic acid that helps in the synthesis of proteins in our
body.
There are three main types of RNA o
Messenger or mRNA
mRNA encodes the amino acid sequence of one or more
polypeptides specified by a gene or set of genes
o Transfer or tRNA tRNAs read the information coded in the
mRNA and transfer the appropriate amino acids to a growing
polypeptide chain during protein synthesis
o Ribosomal or rRNA. rRNAs are constituents of ribosomes that
synthesize proteins. The nucleotides forming RNA consist of the following
components:
1. A nitrogenous base which may be either a purine (adenine or
guanine) or a pyrimidine (cytosine or uracil).
2. Ribose which actually is D-ribose. 3. Phosphoric acid.

6. What is Somatotropin? Explain its Physiological Importance.

Human growth hormone is a hormone of the anterior pituitary gland and is also known as
somatotropin or somatotropic hormone (STH). Its basic function is to cause body cells to grow.
Physiological Importance
1. Effects on protein metabolism:
 GH has predominately anabolic effects on skeletal and cardiac muscles. It stimulates the
synthesis of protein, RNA and DNA.
 It promotes amino acid entry into cells, as does insulin.
 It decreases the catabolism of protein because G.H mobilize free fatty acids to supply energy.
2. Effects on carbohydrate metabolism: (Hyperglycemia)
 GH is a diabetogenic hormone. Because of its anti-insulin effect, GH has a tendency to cause
hyperglycemia.
3. Effects on fat metabolism:
 GH has an overall catabolic effect in adipose tissue.
 It stimulates the mobilization of fatty acids from adipose tissue, leading to decreased
triglycerides
content in fatty tissue and increased plasma levels of fatty acids and glycerol.

4. Effects on inorganic metabolism:

 GH increase the retention of the phosphorus and Ca++ in body fluids by increasing absorption
from the GIT and renal tubules.
 It also causes the retention of Na+, K+, Cl‾ and Mg++.
5.Effects on bone, cartilage, and soft tissues:
 It acts on cartilage and bone, stimulating growth.
 Increases the deposition of connective tissue
7. What are the main physiological functions of Testosterone.

This is the principal hormone of the testes which consists of 19 carbon atoms.
Actions of testosterone
1. Effect on the male reproductive system
 During intrauterine life testosterone is secreted by the genital ridge. Later on, it is secreted by
the placenta. At this stage it causes the development of male sex organs.
 In adult’s testosterone is secreted by the testes. This hormone causes the enlargement of the
male sexual organs, increasing spermatogenesis and maintaining the motility and fertilizing
power of sperm.

2. Effects on secondary sex characteristics

Body hair: Increased growth of hairs on the face, chest, Axilla.
Baldness: Decreased growth of hairs on top of the head.
Voice: Testosterone causes hypertrophy of the laryngeal mucosa and enlargement of the larynx.
It also increases the length and thickness of the vocal cords; the voice becomes deeper. Skin:
Testosterone causes thickness of the skin, roughness of the subcutaneous tissue, deposition of
melanin in skin.
Behavioral changes: Testosterone is also responsible for aggressive moods, active attitudes,
and interest in the opposite sex.
3. Effect on CNS
Increases the libido by directly acting on CNS.
4. Effect on bone
a) Increases thickness of bones. (Major Effect on pelvis)
b) Increases total quantity of bone matrices.
c) Increases the deposition of calcium salts in bones
5. Effect on BMR
It increases the BMR (12-16%) due to increased protein formation.
6. Effect on RBCs Testosterone increases the number of RBCs (15- 20%).

8. Explain Estrogen effect on reproductive System. Estrogen is

a female sex hormone. An 18-carbon steroid.

Types: The naturally occurring estrogen is of three

types: i. 17- β - estradiol ii. Estrone
iii. Estriol

Actions of estrogens
A. Effects on reproductive system: 1.

Effects on the vagina

o Increases the size of the vagina by enlargement of the musculature of the walls of the vagina.
o Changes the simple cuboidal epithelium to stratified epithelium, which is more resistant to
trauma and infection. o Increases the deposition of glycogen. 2. Effects on external genitalia

o Increases the size of the clitoris and labia minora.

o Increases the deposition of fat on the mons pubis and labia majora.

3. Effects on cervix

o Causes slight enlargement of cervix.

o Increases the alkaline secretion of the cervix to neutralize the acidic pH of the vagina.

4. Effects on the uterus

 Increases the size of the uterus.

 Increases vascularity.
 Increases glycogen contents.
 Increases the sensibility of myometrium to oxytocin

5. Effects on the fallopian tubes

 Causes the proliferation of glandular tissue.

 Helps in fertilization by causing peristaltic contraction B. Effects on

secondary sexual characteristics:

1. Effects on breast:

 Promotes the development of the tubular duct system.

 Increases the deposition of fat.
2. Effects on the skin:
Increases vascularity of the skin. Causes softness and smoothness of the skin
3. Effects on the voice: The larynx of a female retains its prepubertal so size the voice
remains high pitched.

C) Other effects:

1. Effects on protein metabolism:

 Increases the synthesis and deposition of proteins.

1. Effects on fat metabolism:
 Increases the synthesis of fat.
  Increases the deposition of fat in subcutaneous tissue, especially the breasts, medial side of
the thigh, and buttocks.
2. Effect-, on water and electrolytes:

It increases the retention of Na+, Of, and water, increasing the E.C.F.

9. Explain factors affecting enzyme activity.

1. Enzyme concentration
The rate of reaction is directly proportional to the concentration of enzyme Enzyme concentration in
the body may fall or rise due to changes in the rate of its synthesis and /or degradation which are brought
about many factors including hormones and metabolites.
2. Substrate concentration
The rate of reaction is directly proportional to the concentration of substrate up to the limit.
3. Effect of temperature
The rate of reaction increases with increase in temperature over limited range of temperature and on
reaching a certain high temperature the enzyme activity starts decreasing Usually the enzyme reaction
in man occur best at or round 37◦C which is the average normal body temperature.

4. Effect of pH
Optimum PH is at which enzyme catalyzes the reaction at maximum rate. e.g. Optimum PH of salivary
amylase is 6.4 to 6.9 and that of trypsin is 8.0 to 9.0. Extreme changes in pH may actually denature the
enzyme. 5. Presence of cofactors, coenzymes and prosthetic groups are also essential for enzymatic
activity.

9. Define enzymes. Explain classification with suitable examples.

Sr. Class Type of Reaction Catalyzed

No

1 Oxidoreductases These enzymes catalyze oxidation – reduction reaction by transferring H atoms or

hydride [H-] ions. 1.Oxidases 2. Dehydrogenases 3. Hydro peroxidases 4.
Oxygenases
2 Transferases These enzymes bring about a transfer of functional group such as phosphate, amino,
acyl, methyl, from one molecule to another molecule.

TYPES.
Transaminases 2. Phosphotransferases (Kinases) 3. Transmethylases 4. Transpeptidases
5. Transacylases
3 Hydrolases These enzymes catalyze hydrolysis (added water is instant decomposed & functional
group of substrates transferred to water)

Subgroups

1. Protease 2. Carbohydrases 3. Lipid hydrolyzing enzymes 4. Deaminases 5.

Deamidases

4 Lyases These enzymes catalyze the addition of NH3, H2O OR CO2 to double bonds or
removal of these groups leaving behind double bonds.

Fumaric acid +H2O ↔ Malic acid (Fumarase enzyme is involved in this Rx).
5 Isomerases These enzyme catalyze the structural change in a molecule by the transfer of group in it
& formation of isomeric form of subsrate.
e.g. Glucose 6-phosphate → fructose 6-phosphate (The enzyme is phosphohehexose
isomerase)

6 Ligases Ligase is an enzyme that catalyzes the binding of two molecules.

Acetyle-coA → Molonyle-coA (Acetyl-CoA carboxylase)

Chapter # 4
Vitamins
1. Chemistry, sources, RDA, biochemical functions and deficiency manifestation of Vit A.
Chemistry o The precursor or/provitamin "A" is the carotenoid pigment of certain
plant known chemically as carotene.
o Carotene is a hydrocarbon.
o Vitamin A is quite heat stable but it is destroyed at high temperatures
in the presence of O2 and air
o The relationship between Retinol, Retinal, and Retinoic acid is as
follows:
Oxidation Retinol → Retinal → Retinoic acid Reduction
Sources Animal origin
• Retinol • Retinal • Retinoic Acid ➢
Animal kingdom. Liver oils of certain species of fish e.g. halibut, shark
and Cod. Also occur in the livers of other animals, egg yolk, butter, cheese,
whole milk, kidney and muscles.
Plant origin
• Carotene • Carotene (most efficient) • Carotene
Carrots, yellow corn, sweet potato, turnip, peaches and spinach.
RDA The Recommended Dietary Allowance (RDA)
900 micrograms (mcg) for adult men and 700 mcg for adult women.
Biochemical 1. Eyes
functions Vitamin a is actively involved in the maintenance of normal visual process
of eye. Retinal occurs in the retina. Vitamin A is a component of visual
pigments of rod and cone cells. It combines with protein opsin to form
rhodopsin which is essential for rod vision in dim light. Vitamin _ A
participates both in dark/light vision as well as in color vision.
2. Reproduction
Retinol and Retinal forms of vitamin A are concerned with the normal
Reproduction.
 Male they facilitate the process of spermatogenesis.
 Female they prevent fatal resorption.

3. Antioxidant role of B carotenes

These trap organic peroxide free radicals within its structure at low 02
concentration as compared to Vitamin E).
4. Bones and teeth
It is essential for the normal growth and Development of bones and teeth.
In some way it is construction of bones and teeth and also rates the process
of mineralization.
5. Enhancement of immune system
Prevention of Infections Vitamin A enhances the activity of immune
system.
 Deficiency 1. Eyes
Serious problem of the vision and eyes are found in various degrees of
deficiencies of vitamin “A”
a. Nyctalopia Night blindness due to disturbance in visual cycle. b.
Xerophthalmia
• Dry cornea, and mucous membranes of eye
• Atrophy of corneal epithelial cells
• Absence of tears • Irritation to blinking
c. Keratomalacia
• Keratinization and degeneration of cornea -Defective vision.
Change in normal epithelium of cornea and conjunctiva
2. Skin
Skin become dry, scaly and thick keratinized. o
Acne
o irregular skin Follicular hyperkeratosis (Excessive development of
keratin in hair follicles)
o Psoriasis 3. Reproduction Male:
o Atrophy of germinal epithelium of testis.
o Digospermia. (Low sperm count)
Female o Disturbance in menstrual
cycle
Toxicity • Acute: Headache, nausea and vomiting.
• Chronic: Dry skin, cracking of lips, bone pain, fragility, brittle nails,
hair Loss, gingivitis, hepatomegaly, ascites and portal hypertension

2. Chemistry, sources, RDA, biochemical functions and deficiency. manifestation of Vit D.

Vitamin D is a fat soluble vitamin. Its deficiency may cause rickets in children and
osteomalacia in adults.
a. Chemistry
These are sterols, which are precursor of Vitamin D. There are about 10 compounds of
Vitamin D out of these only 2 have anti-ricketic property e.g ergosterol and calciferol. b. Source
 Cod and other fish liver oils are best sources, the few rich sources are liver of the animals which
feed fish, eggs, butter, fortified milk .
 D3 content of milk depends on exposure to sunlight. Vitamin - D formed in the skin of human
beings by ultraviolet rays.
 c. Functions of Vitamin – D
1. Absorption of calcium in gut

Vitamin D promotes the Ca++ absorption from the intestine by:

 Increase the formation of Ca++ binding proteins in the

intestine.
 Increase formation of Ca++/ H+ ATPase pump in intestinal
cells.
2. Phosphate absorption
Intestinal absorption of phosphate is increased by Vitamin D.
Serum Ca++ Level Vitamin D, maintains the serum Ca++
level by
 Increased intestinal Ca++ absorption.
 Increase the mobilization of Ca++ from old bones.
 By increasing reabsorption of calcium and phosphate from
renal proximal convulated tubule.
3. Growth of bones
Promote endochondral growth of long bones. Normal levels of calcium and phosphate favor
bone mineralization. It ensures that Ca+ is deposited in the bones.
4. Parathyroid activity
Activity of parathyroid hormone is stimulated in Vitamin D deficiency.
Hypercalcemia: Decreased the activity of parathyroid gland. Hypocalcemia:
Increased the activity of parathyroid gland
5. Teeth
Vitamin D helps in normal teeth formation, if vitamin D is lacking malformation of teeth
occurs. Such as:
• Cavity formation • Hypoplastic teeth • Defective enamel & dentine formation

Effect of Vitamin -D deficiency

Deficiency of vitamin D may cause rickets in children and Osteomalacia in adults.
1. Rickets
It is a disease primarily due to a deficiency of dietary intake of vitamin D but an inadequate
supply of calcium, phosphorus and sunlight may also play a part. The deficiency of vitamin D
results in a lowered calcium level which stimulates the secretion of PTH which acts to restore
the plasma calcium at the expense of bone calcium.
a. Bones become weak and fragile
b. Newly laid bone is un-calcified (RDA)
c. Various skeletal deformities; - 15-20 ug
e.g.
▪ Bow legs: Tibia bends forward.
 ▪ Rickety rosary: Nodule develops at costochondral junction at wrist, ankles and knees. ▪
Kyphosis: backward protrude spine ▪
Lordosis: Side ward spine. Toxicity of Vitamin – D
Nausea, anorexia, vomiting, polyurea,
▪ Scolosis: Front ward spine.
polydipsia.
G.I.T
2. Osteomalacia "Adult Rickets" disturbances.
. Kidney stones formation.
1. It mostly occurs in women who have
little exposure to sunlight and are economically poor and undergone repeated pregnancies and
lactation.
2. Bone minerals are mobilized,.Ca mobilization is greater than Pi mobilization.
3. Bones are soft, weak and easy to get fracture.
4. Bowing of legs (bending of lower leg bones).
5. Muscular weakness: patient will find difficulty in climbing stairs and getting out of chair. •
Spontaneous fracture or collapse of vertebra are common.
6. Tetany may be manifested by "carpopedal spasm" and facial twitching

3. Give an account of sources, chemistry, functions, RDA and deficiency manifestations of

ascorbic acid (Vit C).
a. Chemistry
RDA :60mg
 In human body vitamin C is found as L- Ascorbic Acid.  The
active form of vitamin C is ascorbate acid  Human body is unable
to synthesize Vitamin - C.
 It is a strong reducing agent and therefore readily oxidized in the body to dehydro
ascorbic acid.
b. Source o
Plant Source
Fresh Fruits: orange, lemon, grapes, guava, apple, strawberry.
Fresh Vegetables: tomatoes, cauliflower, onion, lettuce, green peas, beans etc.
o Animal Source
Liver, kidney, adrenal gland

1. Intercellular substance
Ascorbic acid is required for the functional activities of fibroblast and osteoblast and for the
formation of collagen fibers and connective tissues.

2. Wound repair
Vitamin C takes active part in wound repair. It lays down the connective tissue which helps in
healing of wound.
 The deficiency of Vitamin C results in a disease called
scurvy Haemorrhage
Teeth become lose and fragile
Follicular hyperkeratosis
Retardation in the growth of bone
3. Hematopoiesis
Vitamin C has a stimulating effect on hematopoiesis, because anemia usually accompanies scurvy.
4. Antioxidant
It prevents injury to the body tissues from the toxic oxidation products.
5. Iron absorption and mobilization
Vitamin C helps in reducing Fe3+ to Fe2+ and helps in the absorption of iron from the intestine
and its utilization (iron is absorbed in Fe2+ form).
6. Conversion of folic acid
It is involved in the conversion of folic acid to its active form called tetra hydrofolate. Ascorbic
acid also inhibits the oxidation of tetrahydrofolate. Its deficiency causes megaloblastic anemia due
to non-utilization of folic acid.

Toxicity.
Oxidative damage Erythrocytes of premature infants Excess
ascorbic acid excretion e give a false +Ve test for
sugar
oxalate stones.

4. Chemistry, sources, RDA, biochemical functions and deficiency manifestation of:

a) Vitamin B6 b) Vitamin B9 c) Vitamin B12 d) Vitamin B2 e)
Vitamin B3 f) Vitamin B7
Type of Chemistry Sources Functions Deficiency RDA
Vitamin

Vitamin B2 Vitamin B2 Animal 1. Oxidation- Mouth Lesions: Involve

(Ariboflavinosis) is a liver kidney heart Reduction: tongue, glottis, pharynx 1.7
water-soluble heat fish eggs Riboflavin as such is not Weakness, drowsiness, mg
stable vitamin a. milk Plant biologically active, in Lassitude.
Riboflavin Fresh fruits root order to activate it must be Cheilosis: Lesions at the
vegetable phosphorylated, which angles of mouth.
b. Lactoflavin
takes place mainly in
like carrot Angular Stomatitis
kidney and intestinal wall fissures at the corners of
Intestinal
Bacteria lips.
Dermatitis
Skin becomes scaly,
greasy and inelastic
Vitamin B3 NIACIN is pyridine Animal: 1. Act as Co-Enzyme.
3- Carboxylic acid. Liver, Kidney, It acts as "H" acceptor in
In animal tissues it is Meat, Fish, various "Redox" reaction Pellagra 19mg
found as amide form Eggs, Milk in the form of NAD &
called NADP. They worked with
Plants:
"Niacinamide" Dried yeast, dehydrogenases, and act
dried legumes as"H"acceptor Coenzyme.
whole wheat,
peanuts,
tomatoes.

2. Decreased
blood
Cholesterol Level
Niacin is supposed to
involve by some
biochemical processes to
lower the cholesterol level.
3. Act as
CNS
stimulator
It has stimulatory effect on
CNS.
4. Vasodilator
Niacin is good vasodilator
and Produces flushing
which is accompanied
with burning and itching
sensation

Vitamin B6 Vitamin be is water Plant 1. Decarboxylation 1. Hypochromic

soluble, heat stable Whole 2. Transamination microcytic anemia
vitamin Pyridoxine grains, Oxaloacetate glutamate as 2. Lymphocytopenia and
Pyridoxamine. cabbage, legume, parate + ketoglutarate Leukemia
Pyridoxa cauliflower 3.
3. Deamination Growth retardation 2mg
Animal: 4.
Serine——Pyruvate+
Egg yolk, meat, NH3 5. Dermatitis
Peripheral
fish, milk, yeast 4. Condensation neuritis
Glycine + Succinyl CoA— depression
——>daltaamino
levulinic acid
5. Glycogen
phosphorylase It appears
to be the part of molecule
of glycogen
phosphorylase
 Vitamin B7 Biotin is water Animal: 1. It acts as co-enzyme 1. Lassitude
soluble, heat stable Liver, kidney, for various 2. Anemia.
Vitamin H milk eggs carboxylation 3. Increase Cholesterol
Co-enzyme R Plants: reactions, level.
Fruits, tomatoes2. it is involved in the 4. Muscular pain. 25ug
vegetables, formation of Carbonyl 5. Dermatitis.
phosphate from NH3 6. Growth Retardation
and CO2 and ATP in
urea cycle, it takes part 7. Fall of hairs
in the biosynthesis of
purine and lipid in
certain animals.
3. It catalyzes the
deamination reaction
of threonine, serine
and aspartic acid.
Vitamin B9 1. The active Animals: 1. The most important 1. Haemopoietic defects:
form of folic acid is Liver, kidney, function of folic acid is to Bone marrow depression.
tetrahydrofolate beef. carry out reactions •Pancytopenia.
2. Its structure Plants: involving transfer of one • Megaloblastic anemia.
has three components Cauliflower, wheat "C" moiety such as: a) 2. Reproductive defects.
has__ A pteridine and root Formyl - CHO Azoospermia
nucleus linked to Para vegetables. b) Methyl - CH3 2.
amino benzoic acid to amenorrhea. 400600
2. It is involved in the 3. Growth retardation
form pteroic acid. This ug
synthesis of choline.
in turn is linked to
glutamic acid. 3. It regulates the
3. F.A is reduced, process of haematopoeisis
first to 7. dihydrofolic along with vitamin –B12
acid and then to 4. Maintain normal
tetrahydrofolate growth and development.
5. It has a significant
role in histidine metabolism.
Vitamin B12 Naturally 1. Erythropoiesis Pernicious Anemia
occurring 2. W.B.C maturation 1.Pernicious anemia is
organic compound, Microorganisms It is required for the normal failure of the absorption of
contains cobalt. It is Animal origin maturation of WBC and vitamin B12 rather than
water soluble Liver and kidney thrombocytes dietary deficiency.
whole milk, eggs 3. Protein synthesis 2.Failure of intrinsic factor
Heat stable at neutral
fish cheese and Vitamin B12 activates amino secretion or from 2.4
PH but not at alkaline
muscle. acid for the synthesis of production of anti-intrinsic ug
PH
Not present in protein factor antibodies.
Two different types of
4. Isomerization Rx 3.The anemia of vitamin
vitamins B12 that are plants
B12 deficiency is really
used in therapeutics Various isomerization
due to tissue folic acid
are: reaction is influenced by
deficiency.
Hydroxocobalamin cobalamin
4.B12 deficiency impairs
Cyanocobalamin 5. Folate Recycling the metabolism of folic
By transmethylation acid that disrupts
6. Lipotropic factor erythropoiesis, causing
Vitamin B12 has lipotropic immature precursors of
effect and regulate over all erythrocytes
metabolism of fat (Megaloblastic anemia).
6. Synthesizing effect It has
synthesizing role in lipid
nucleic acid amino acids and
various other substances.

Chapter # 5
Biotechnology
1. Describe briefly about Genetic Engineering.
It is a set of technologies used to change the genetic makeup of cells, including the transfer of
genes within and across species boundaries to produce improved or novel organisms.
Concept of Genetic Engineering
Main idea of genetic engineering: DNA of one organism can express its characters in
another organism also. Process of Genetic Engineering The important tools of genetic
engineering: o Enzymes o Vectors
o cDNA clone bank or cDNA library o
gene bank or genomic library.
2. Describe importance of Biotechnology.
1. Development of new drugs’ chemotherapeutic agents
2. Advancement in drug therapy by using hybridoma technology, recombinant DNA technology,
tissue culture and cell culture technology and gene therapy.
3. Used in hormone replacement therapy for the persons who are deficient in a particular
hormone.
4. Used in tissue culture technology, the plant cells or tissues are grown in a test tube or a conical
flask. The grown-up cell line can be used for elimination of pathogens from plants and for
improvement of crops and their respective yield.
5. Improved treatments for many of the diseases. It has helped in the development of better
vaccines to control the spread of infectious diseases.
6. Revolution in the diagnosis of many epidemic diseases.