Question : What are the subgroups of redox enzymes?

redox enzymes or oxidoreductases are divided into 4 sub-groups: oxidases dehydrogenases

hydroperoxidases oxygenases

Question : What do you understand by the term riboenzyme?

Ribozymes (ribonucleic acid enzymes) are RNA molecules that are capable of catalyzing specific biochemical
reactions, similar to the action of protein enzymes.

Question : Write a note on the following.

Substrate: The substance on which the enzymes act to convert them into product.The reactant in biochemical
reaction is termed as substrate.When a substrate binds to an enzyme it forms an enzyme-substrate
complex Apoenzymes: enzymes with its cofactor removed is known as apoenzymes. It is inactive enzyme and
require co-factor for activation.Cofactor: Co-factor is the non protein molecule which carries out chemical
reactions that can not be performed by standard 20 amino acids.Holoenzyme: Apoenzyme together with its
cofactor. The complete complex of a protein with all necessary small organic molecules, metal ions and other
components is termed as holoenzyme of holoprotein.

Question : Write a note on the structure of enzymes.

Structure of enzymes:The active site of an enzyme is the region that binds substrates, co-factors and
prosthetic groups and contains residue that helps to hold the substrate.Active sites generally occupy less than
5% of the total surface area of enzyme.Active site has a specific shape due to tertiary structure of protein.A
charge in the shape of protein affects the shape of active site and function of the enzyme.

Question : Discuss the Properties of enzymes.

Properties of enzymes:Catalytic propertyEnzymatic propertySolubilitySpecificityProtein
NaturePHTemperatureCatalytic property: Small amount of enzyme can catalyze the large amount of substrate
in biological reactions.Enzymatic property: The velocity of enzymatic reaction increase as the concentration of
up to certain maximum but after certain period of time it decrease.Solubility: Enzymes are mostly soluble in
water and dilute alcohol solution. The enzyme can precipitate in concentrated alcohol, ammonium sulphate,
acetic acid.Specificity: Enzymes are specific in nature and catalyze a specific reaction.Protein in Nature: All
enzyme are protein in nature with large molecular weight.PH: Acids deactivates / destroy those enzyme that
act at alkaline PH. E.g: Trypsin (an important enzyme secreted by pancrease and very important for proper
digestion of food). While base deactivates those enzymes that act at acidic PH. E.g: PepsinTemperature:
Optimum temperature for enzyme activity is 35oC to 40oCAt 0oC it become inactiveAt 10oC to 20oC = little
activityAt 35oC to 40oC = Maximum activityAt 50oC = InactivateAt 600oC = Destroy

Question : Write the names of water soluble vitamins.

Vitamin AVitamin DVitamin EVitamin K

Question : Name thermo-labile vitamins.

Thiamine (Vitamin B1)Antithetic acid ( Vitamin B3)

Question : Write the other names of Vitamin A.

RetinolRetinal Retinoic acid

Question : What is the antioxidant role of beta carotenes?

beta carotenes trap the organic peroxide free radicals within its structure at low oxygen concentrations as
compared to vitamin E that acts at high oxygen concentrations.

Question : How vitamin A is involved in immune system activities?

Vitamin A enhances the activity of immune system. Vitamin A deficient children are susceptible to
complications of measles. Mild deficiency leads to increased susceptibility to infectious diseases.

Question : What are the symptoms of keratomalacia?

The symptoms of keratomalacia includes: Keratinization and degeneration of cornea -Defective
vision. Dryness Thickness Change in normal epithelium of cornea and conjunctiva

Question : What are the other names of vitamin D?

CalciferolErgosterol.Anti-ricketic Vitamin
Question : What is 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. Rickets is also seen clinically when there is a defect in the
conversion to calcitriol.

Question : Why osteomalacia is common in females?

It mostly occurs in women who have little exposure to sunlight and are economically poor and undergone
repeated pregnancies and lactation. Bone minerals are mobilized, X-ray shows less dense and less
mineralized bones.Ca mobilization is greater than Pi mobilization. Bones are soft, weak and easy to get
fracture.

Question : What are the common characteristics of osteomalacia?

The most common features of osteomalacia are:Looser's Zones is the characteristic radiographic feature.
Muscular weakness--- patient will find difficulty in climbing stairs and getting out of chair. Spontaneous
fracture or collapse of vertebra are common. Tetany may be manifested by "carpopedal spasm" and facial
twitching.

Question : What do you know about Vitamin E?

Vitamin E is a fat soluble vitamin. It is most important vitamin to maintain the normal process of reproduction.
The origin of the name tocopherol is from ?tocos? meaning childbirth and ?phero? meaning to bear, implying
a substance which increases fertility.

Question : Name the plant & animal sources of Vitamin E?

Animal sources: Egg yolk, milk, liver, cheese, butter Plant sources: Wheat germ oil, cotton seed oil, peanut oil

Question : Name the diseases in which the treatment with Vitamin E

is helpful.
The diseases in which the treatment with Vitamin E is helpful include:Nocturnal muscle crampsIntermittent
claudication Fibrocystic breast disease Atherosclerosis
Question : What are the abnormalities caused by Vitamin E
deficiency?
The abnormalities caused by Vitamin E deficiency are:Haemolysis OedemaMuscular dystrophy Reproduction
failureTesticular dystrophy and defective spermatogenesis in males Infertility due to abnormalities in
menstrual cycle Abortion Liver necrosisPremature infants.

Question : What is Coagulation Vitamin?

The name vitamin K stands for Coagulation vitamin given by scientist to a substance that prevented
Haemorrhage. Its deficiency is characterized by hypoprothrombinemia and prolonged prothrombin time.

Question : What are the different chemical forms of vitamin K?

Chemically there are three forms of vitamin K: K1 (Plant Origin): Phylloquinone, isolated from alfalfa
plant. K2 (Bacterial Origin): menaquinone.franoquinone K3 (Synthetic product) Menadione : converted in
the body to one of menaquinones or phylloquinone.

Question : Name the blood clotting factors.

Factor II ( prothrombin)Factor VIIFactor IXFactor X

Question : What are the causes of hemorrhage in new borns?

Inadequate intake of Vitamin K by mother during pregnancy. Congenital absence of E-coli bacteria in the G.I.T.
Decreased permeability of placenta for Vitamin K during gestation

Question : Name the drugs having anti-vitamin K activity?

Drugs having anti-vitamin K activity include: HeparinWarfarin Dicumerol

Question : What are the animal & plant sources of Vitamin C?

Plant Sources: orange, lemon, grapes, guava,apple, strawberry, tomatoes, cauliflower,cabbage, onion,
lettuce, green peas, beans etc. Animal Sources: Animal tissues are not a good source. Liver, kidney, adrenal
glands contain Vitamin C.

Question : What is scurvy?

Scurvy is a condition characterized by general weakness, anemia, gingivitis (gum disease), and skin
hemorrhages caused by a prolonged deficiency of vitamin C (ascorbic acid) in the diet. Vitamin C plays a
crucial role in the formation of collagen, a major component of connective tissue.

Question : What is the role of Vitamin C in protein Matrix synthesis?

It helps in the synthesis of protein matrix i.e by synthesizing collagen and hydroxyproline. It also play an
important role in certain amino acid metabolism such as phenylanaline and tyrosine

Question : What are the other names of Vitamin B1?

Aneurine Thiamine Anti - Beri Beri factor Anti Neuritic factor

Question : What are the plant sources of Vitamin B1?

It occurs in the outer layer of grains like bran and rice polishings. it is found in whole cereal, yeast, whole
wheat flour, pulses , nuts and fresh fruits. Vegetables contain it to a lesser extent.

Question : What are the symptoms of riboflavin deficiency?

Mouth Lesions: Involve tongue, glottis, pharynx etc. Weakness, drowsiness, Lassitude. Redness and shiny
appearance of lips Cheilosis : Lesions at the angles of mouth. Angular Stomatitis: painful fissures at the
corners of lips. Dermatitis : Skin becomes scaly, greasy and inelastic

Question : How Vitamin B3 is prepared in laboratory?

In the laboratory Vitamin B3can be prepared by oxidation of "nicotine" with strong oxidizing agent such as
permanganate or fuming nitric acid
Question : Write down the synonyms of Vitamin B6?
Pyridoxine PyridoxaminePyridoxa

Question : What is biochemical role of vitamin B6?

DecarboxylationTransminationDeaminationCondensation

Question : What is the structure of Folic acid?

Folic acid is pteroylmonoglutamic Acid. Its structure has three components. A pteridine nucleus is linked to
Para amino benzoic acid to form pteroic acid. This in turn is linked to glutamic acid.

Question : What are the other names of Vitamin B12?

Cobalamin Cyanocobalamine Cobamide Cobalt aminAntipernicious anemia factor

Question : Which form of vitamin B12 is used in Therapeutics?

Two forms of vitamin B12 are used in therapeutics viz: Hydroxycobalamin (physiological form of
vitamin) Cyanocobalamin (produced during isolation of vitamin)

Question : Which form of vitamin B12 is used in Therapeutics?

Two forms of vitamin B12 are used in therapeutics viz: Hydroxycobalamin (physiological form of
vitamin) Cyanocobalamin (produced during isolation of vitamin)

Question : What is Megaloblastic anemia?

Megaloblastic anemia is an anemia (of macrocytic classification) that results from inhibition of DNA synthesis
during red blood cell production. When DNA synthesis is impaired, the cell cycle cannot progress from the G2
growth stage to the mitosis (M) stage.
Question : What are the clinical features of biotin deficiency?
Deficiency of biotin may cause following clinical features: Lassitude. Anemia. Increase Cholesterol
level. Muscular pain. Dermatitis. Retardation of growth. Fall of hairs.

Question : What are the symptoms of beri beri?

Beriberi, nutritional disorder caused by a deficiency of thiamine (vitamin B1) and characterized by impairment
of the nerves and heart. General symptoms include loss of appetite and overall lassitude, digestive
irregularities, and a feeling of numbness and weakness in the limbs and extremities.

Question : How thiamine acts as carboxylase?

Vitamin B1 plays an Important role in various decarboxylase reactions. e.g; Pyruvic Acid ? Acetyl CO-A + C Citric
Acid ? a-Ketogluteric Acid+CO

Question : What is the role of Vitamin K in Blood clotting?

The most important function of vitamin K is that it helps in the formation of blood clotting factors II(
prothrombin), VII, IX and X by the liver. These factors are formed by liver in presence of Vitamin-K. Vitamin K
is not the structural component of these compounds but bring about postranslational change necessary for
their function.

Question : How does Vitamin E take care of RBCs?

Vitamin E looks after RBCs and prevents them from heamolysis by preventing membrane damage from
various oxidants.

Question : Into how many types Vitamins are classified on the basis
of solubility?
On the basis of solubility Vitamins are classified into two types:Fat-soluble vitaminsWater-soluble vitamins
Question : Write a short note on Vitamins.
Vitamins:A vitamin is an organic molecule (or related set of molecules) that is an essential micronutrient that
an organism needs in small quantities for the proper functioning of its metabolism. OR Organic molecules
needed in very small amounts in natural food stuff that are essential for cellular metabolism. There are 13
vitamins your body needs. They are Vitamin A, vitamin B (thiamine, riboflavin, niacin, pantothenic acid, biotin,
vitamin B-6, vitamin B-12 and folate), Vitamin, Ce Vitamin D Vitamin E, and Vitamin K.

Question : Write the classification of Vitamins.

Classification of vitamins:Vitamins are classified int two categories 1) Water soluble vitamin2) Fat soluble
vitamins1) Water soluble vitamins:Water-soluble vitamins dissolve easily in water and, in general , are readily
excreted from the body, to the degree that urinary output is a strong predictor of vitamin consumption. They
are not stored in the body, so they have to be taken on a regular basis to prevent shortage in the body. Water
soluble vitamins are;Vitamin CVitamin B complex (thiamine, riboflavin, niacin, pantothenic acid, biotin, vitamin
B-6, vitamin B-12 and folate)2) Fat-soluble vitamins:Fat -soluble vitamins are stored in the body's fatty tissue.
They are absorbed through the intestinal tract with the help of lipids (fats).. The four fat-=soluble vitamins
are;Vitamins AVitamin DVitamin EVitamin K

Question : Write a note on functions, sources and deficiencies of

Vitamin A (Retinol).
Vitamin A is a group of unsaturated nutritional organic compounds that includes retinol, retinal, retinoic acid,
and several pro-vitamin A carotenoids (most notably beta-carotene).1. Functions of Vitamin A (Retinol):Helping
vision in dim lightKeeping skin and the lining of some parts of the body, such as the nose, healthy Supports
growth (skeletal growth)Synthesis of certain glycoproteins.Essential for the maintenance of proper immune
system.2. Soureces of Vitamin A (Retinol):Cheese, eggs, oily fish, fortified low-fat spreads, milk and yoghurt,
liver and liver products such as liver pate-(this is rich source of vitamin A, particularly important during
pregnancy)3. Deficiency of Vitamin A (Retinol):Night blindnessKeratinization of epithelial cells Conjunctival
xerosis (The conjuctiva becomes dry and non-wettable)Corneal xerosisFollicular hyperkeratosis, anorexia &
growth retardation

Question : Write a note on function, sources and deficiencies and

Toxicity of Vitamin D.
Vitamin D is a fat-soluble vitamin that is naturally present in very few foods, added to others and available as a
dietary supplement. It is also produced endogenously when ultraviolet rays from sunlight strike the skin and
trigger vitamin D synthesis.Functions of Vitamin D:1. Calicum and Phosphorus HomeostasisCalcium and
Phosphorus absorption (small intestine)Caleium reabsorption (bone and kidney)Maintain blood calcium
levels.2. Bone formation Stimulate calcium uptake for deposition as calcium phosphate (Osteoblasts)3.
HormoneRegulation of gene expressionCell growth2. Sources of Vitamin D:Oily fish, Red meat, Liver, Egg
yolks, Fortified foods and Dietary supplements.3. Deficiency of Vitamin D:Deficiency of vitamin D causes
rickets in children and osteomalacia in adultsCausing enlargement and softening of bonesDelay in teeth
formation The weight bearing bones are bent to form bow-legsDecreased serum calcium4. Toxicity of Vitamin
D:Hypervitaminosis DCalcification of soft tissue

Question : Write a note on functions, sources and deficiencies of

Vitamin E (Tocopherol):
Vitamin E (Tocopherol) is naturally occurring antioxidant. essential for normal reproduction in many animals.
Tocopherol (Greek: tokos-child birth; pheros-bear; ol-alcohol), Anti-sterility vitamin.1. Sources of vitamin
E:Plant sourcesCereal grains especially in germVegetable and seed oils e.G: cotton seed oil, peanut oilAnimal
sourcesMeat, Milk, Butter, Eggs and Liver.2. Function of Vitamin E:Act as Antioxidant.Acts as a co-enzymePlays
a role in agingSexual performanceNecessary for the normal process of reproduction3. Deficiency of Vitamin
E:Reproduction failureDefective spermatogenesis (In male)In female, infertility due to abnormalities in
menstrual cycle.Rupture of RBCs membrane due to increased lipid per oxidationNeurogical problems due to
poor nerve conductionLiver necrosis

Question : Write a short note on Vitamin.

Vitamins:A vitamin is an organic molecule (or related set of molecules ) that is an essential micronutrient that
an organism needs in small quantities for the proper functioning of its metabolism. OR Organic molecules
needs in very small amounts in natural food stuff that are essential for cellular metabolism. There are 13
vitamins your body needs They are Vitamin A, vitamin B (thiamine, riboflavin, niacin, pantothenic acid, biotin,
vitamin B-6, vitamin B-12 and folate), Vitamin C. Vitamin D, Vitamin E, and Vitamin K.

Question : Write the classification of Vitamins

Classification of vitamins:Vitamins are classified into two categories1) Water soluble vitamins2) Fat soluble
vitamins1). Water soluble vitamins:Water-soluble vitamins dissolve easily in water and, in general, are readily
excreted from the body, to the degree that urinary output is a strong predictor of vitamin consumption. They
are not stored in the body, so they have to be taken on a regular basis to prevent shortage in the
body.Vitamin CVitamin B complex (thiamine, riboflavin, niacin, pantothenic acid, biotin, vitamin B-6 vitamin B-
12 and folate)2). Fat-soluble vitamins:Fat-soluble vitamins are stored in the body's fatty tissue. They are
absorbed through the intstinal tract with the help of lipids (fats)... The four fat-soluble vitamins are; Vitamins
AVitamins DVitamins EVitamins K
Question : Write a note on functions, sources and deficiencies of
Vitamin A (Retinol).
Vitamin A is a group of unsaturated nutritional organic compounds that includes retinol, retinal, retinoic acid,
and several pro-vitamin A carotenoids (most notably beta-carotene).1. Functions of Vitamin A (Retinol):Helping
vision in dim lightKeeping skin and the lining of some parts of the body, such as the nose, healthySupports
growth (skeletal growth)Synthesis of certain glycoproteins.Essential for the maintenance of proper immune
system.2. Sources of Vitamin A (Retinol):Cheese, eggs, oily fish, fortified low-fat spreads, milk and yoghurt, liver
and liver products such as liver pate-this is rich source of vitamin A, particularly important during pregnancy)3.
Deficiency of Vitamin A (Retinol):Night blindnessKeratinization of epithelial cellsConjunctival xerosis (The
conjuctiva becomes dry and non-wettable)Corneal xerosisFollicular hyperkeratosis, anorexia & retardation

Question : Write a note on functions, sources and deficiencies and

Toxicity of Vitamin D.
Vitamin D is a fat-soluble vitamin that is naturally present in very few foods, added to others, and available as
a dietary supplement. It is also produced endogenously when ultraviolet rays from sunlight strike the skin and
trigger vitamin Dy synthesis.Functions of Vitamin D:1. Calcium and Phosphorus HomeostasisCalcium and
Phosphorus absorption (small intestine)Calcium reabsorption (bone and kidney) Maintain blood calcium
levels.2. Bone formation Stimulate calcium uptake for deposition as calcium phosphate
(Osteoblasts)3. HormoneRegulation of gene expressionCell Growth2. Sources of Vitamin D:Oily fish, Red
meat, Liver, Egg yolks, Fortified foods and Dietary supplements3. Deficiency of Vitamin D:Deficiency of vitamin
D causes rickets in children and osteomalacia in adultsCausing enlargement and softening of bonesDelay in
teeth formationThe weight bearing bones are bent to form bow-legsDecreased serum calcium4. Toxicity of
Vitamin D:Hypervitaminosis DCalcification of soft tissue

Question : Write a note on functions, sources and deficiencies of

Vitamin E (Tocopherol):
Vitamin E (Tocopherol ) is naturally occurring antioxidant. essential for normal reproduction in many animals.
tocopherol (Greek: tokos-child birth; pheros-bear; ol-alcohol), Anti-sterility vitamin.1. Sources of vitamin
E:Plant sourcesCereal grains especially in germVegetable and seed oils e.g: cottonseed oil, peanut oilAnimal
sources Meat, Milk, Butter, eggs and Liver.2. Function of Vitamin:Act as Antioxidant.Acts as a co-enzymeplays
a role in agingSexual performance Necessary for the normal process of reproduction3. Deficiency of Vitamin
E:Reproduction failureDefective spermatogenesis (in male)In female, infertility due to abnormalities in
menstrual cycleRupture of RBCs membrane due to increased lipid per oxidationNeurogical problems due to
poor nerve conductionLiver necrosis
Question : Write a note on functions, sources and deficiencies of
Vitamin K:
Vitamin K:The only fat soluble vitamin with a specific coenzyme function. Required for the production of blood
clotting factors, essential for coagulation, also known as antihemorrhagic vitamin or Coagulation
vitamin.Chemically there are three forms of vitamin K;1. Vitamin K1 is from plant origin. E.g
Phylloquinone2. Vitamin K2 is from bacterial origin. E.g Menaquinone3. Vitamin K3 is synthetically
preparations. E.g MenadioneFunction of vitamin K:Essential for clotting of blood.Conversion of prothrombin
to thrombin, an active enzymeFormation of fibrinogen to fibrin, leading to clot formation.Prevents some
cardiovascular diseasesPlay important role in bone formationIn plants vitamin K is essential for
photosynthesis.Deficiency of vitamin K:prolong blood cloting timeIncreased bleeding and hemorrhageBlood in
urine or stoolWeakening of bones, osteoporosis and fractureToxicity of Vitamin K:Hypervitaminosis K,
Hyperbilirubinemia, thrombosis, hemolytic anaemia and jaundice, particularly in infants. The toxic effect is
due to increased breakdown of RBC.

Question : Write the names of Water soluble vitamins.

Water Soluble vitamins:Water-soluble vitamins dissolve easily in water and, in general, are readily excreted,
are readily excreted from the body. There are nine water-soluble vitamins which include;Vitamin CVitamin B
complexThiamineRiboflavinNiacinPantothenic acidBiotinVitamin B-6Vitamin B-12Folate (folic acid)

Question : Write a note on thiamine (vitamin B1)

Thiamine (Vitamin B1):Thiamine (vitamin B1) acts as a coenzyme in the metabolism of the body. It is also
known vitamin B1, thiamine, and anti-beriberi factor.Sources of vitamin B1:Egg yolk, Liver of fish, Milk, Cereals
(food grains), Pulses, Vegitables etc.Functions of vitamin B1:Essential for normal growth and development of
body like other vitaminsTreatment of beriberiCoenzyme needed for glucose breakdown of glucose to provide
energy Important for nerve function because:Glucose is nerve cell energy sourceNeeded for synthesis of
neurotransmitters (chemical signals form neurons)Act as Co-enzymes:Bind enzymes to promote their activity
Carriers of electrons, atoms, or chemical groups that participate in the reactions Organic non-protein
molecule examples: B vitaminsDeficiency of vitamin B1:Beriberi: Weakness, nerve degeneration, Heart
changes Depression Enlarged heart, cardiac failureMuscular weaknessAbdominal pain

Question : Write a note on Riboflavin (vitamin B2).

Riboflavin:Riboflavin is a vitamin that is needed for growth and overall good health. It helps the body break
down carbohydrates, proteins and fats to produce energy, and it allows oxygen to be used by the body. It is
water soluble and heat stable vitamin.Sources of Riboglavin (vitamin B2):Milk products (yogrut, cheese), whole
grains, Liver, Eggs, Carrot, Also synthesized by intestinal bacteria.Functions of Riboflavin (vitamin B2):To
produce ATP from carbohydrate, fat, and proteinInvolved in converting folate, niacin, vitamin B6 and vitamin K
into their active formsFor eye conditions i.e; eye fatigue, cataracts and glaucoma.Deficiency of Riboflavin
(vitamin B2):injuries heal poorlymouth ulcerssore throateye burning, tearing, itching

Question : Write a note on Niacin (Vitamin B3):

Niacin:Niacin, also known as nicotinic acid, is an organic compound and a form of vitamin B3, an essential
human nutrient. It has the formula C6H5NO2. It is water soluble and thermostable vitamin its deficiency is
charcterized by pellagra. It is also known as Nicotinic acid, Niacinamide, Vitamin B3.Sources of Niacin (Vitamin
B3):Milk, eggs, meat, poultry, fish, cereals, Nuts, Leafy vegetable.Functions of Niacin (Vitamin B3):Synthesis of
fatty acids and cholesterolCNS stimulatorEssential for normal growth and development of body like other
vitamins.Deficiency of Niacin (Vitamin B3):Diarrhea, abdominal pain, vomitingPellagra, decreased appetite,
indigestion,Inflamed, swollen, smooth, bright red tongueDepression, apathy, fatigue, loss of memory,
headacheBilateral symmertical rash on areas exposed to sunlight

Question : Write a note on Biotin (vitamin B7).

Biotin:Biotin is a water-soluble B vitamin, also called vitamin B7 and formerly known as Vitamin H or
coenzyme R. It is involved in a wide range of metabolic processes, both in humans and in other organisms,
primarily related to the utilization of fats, carbohydrates, and amino acids.Sources of Biotin (vitamin B7)Meats,
egg yolks, soybeans, fish, whole grains, fruits, vegetables. Also produced by G1 bacteria.Functions of Biotin
(vitamin B7):Part of a coenzyme used in energy metabolism, fat synthesis, amino acid metabolism, and
glycogen synthesis.Deficiency of Biotin (vitamin B7):Depression, lethargy, hallucinations, number or tingling
sensation in the arms and legsRed, scaly rash around the eyes, nose, and mouthAnemiaHair loss

Question : Write a note on Pantothenic Acid (vitamin B5).

Pantothenic Acid (vitamin B5):Pantothenic acid, also called vitamin B5 or pantothenate, is a water-soluble
vitamin. Pantothenic acid is an essential nutrient. Animals require pantothenic acid in order to synthesize
coenzyme-A(CoA), as well as to synthesize and metabolize proteins, carbohydrates, and fats.Sources of
Pantothenic Acid (vitamin B5):Widespread in foods, Organ meats, Mushrooms, Avacado. Broccoli, Whole
grainsFunction of Pantothenic Acid (Vitamin B5):Part of coenzyme A, used in energy metabolismSynthesis of
coenzyme ACarbohydrate, fatty acid, and amino acid breakdown Synthesis of neurotransmitters, steroid
hormones, and hemoglobinDeficiency of Pantothenic Acid (vitamin B5):Vomiting, nausea, stomach
crampsInsomnia, fatigue, depression, irritability, restlessness, apathyHypoglycemia, increased sensitivity to
insulin
Question : Write a note on Vitamin B6.
Vitamin B6:Vitamin B6 refers to a group of chemically similar compounds which can be interconverted in
biological systems. Vitamin B6 is part of the vitamin B group of essential nutrients. It is also known as
Pyridoxine, Pyridoxal, Pyridoxamine.Sources of Vitamin B6:Potatoes, legumes, noncitrus fruits, Fortified
cereals, Liver, Meats, fish, poultry.Functions of Vitamin B6:Helps to convert tryptophan to niacin and serotonin
and helps to make red blood cellsDeficiency of Vitamin B6:Scaly dermatitisMouth and tongue soresAnemia
(small-cell type)Depression, confusion, abnormal brain wave pattern, convulsions

Question : Write a note on Folate (folic acids).

Folate (folic acids):Folate, distinct forms of which are known as folic acid, folacin, and vitamin B9, is one of the
B vitamins. It may be taken by mouth or by injection. The recommended adult daily intake of folate in the U.S.
is 400 micrograms/day from foods or dietary supplements. Other names of folate are; Folic acid, Folacin,
Pteroylglutamic acid (PGA).Sources of Folate folic acids):Fortified grains, enriched grans, vegetables, legumes,
seeds, Liver, yeast, NutsFunctions of Folate (folic acids):Folate coenzymes needed for DNA synthesis.Important
in early pregnancy for neural tube formation.Prevent heart disease.Deficiency of Folate (folic acids):Neural
tube defects including spina bifida, poor growth, macrocytic or megaloblastic anemia, nerve development and
function problems, diarrhea, tongue inflammation, reproductive defects,fatigue, increased risk of heart
disease and some cancers

Question : Write a note on Vitamin B12 (cobalamin).

Vitamin B12 (cobalamin):Vitamin B21, also known as cobalamin, is a water-soluble vitamin that is involved in
the metabolism of every cell of the human body. It is a cofactor in DNA synthesis, and in both fatty acid and
amino acid metabolism. It is also known as cobalamine, cyanocobalamine, anemia factor.Sources of Vitamin
B12 (cobalamin)Animal products (meat, fish, poultry, shellfish, milk, cheese, eggs) Fortified cereals
etc.Functions of Vitamin B12 (cobalamin):Helps to maintain nerve cells Protein synthesis WBCs
maturationsErythropoiesisDeficiency of Vitamin B12 (cobalamin):Pernicious anemia, increased homocysteine,
decreased folate activation, numbness and tingling, gait abnormaltities, memroy loss, disoriention, paralysis,
death

Question : Write a note on Vitamin C.

Vitamin C: Vitamin C, also known as ascorbic acid and L-ascorbic acid, is a vitamin found in various foods and
sold as a dietary supplement. It is used to prevent and treat scurvy. It is water soluble, White crystalline,
odorless and sour taste vitamin.Sources of Vitamin C:Cirturs fruits, Cabbage-type vegetables, dark green
vegetable (such as bell peppers and broccoli), Cantaloupe, strawberries, Lettuce, tomatoes, potatoes, Papayas,
mangoesFunctions of Vitamin C:Collagen synthesisAntioxidantAmino acid metabolismSynthesis and
maintenance of collagen, the base of all connective tissueHelps maintain the immune systemRegenerates
active antioxidant form of vitamin E.Deficiency of Vitamin C:ScurvyAnemia (small-cell type)Atherosclerotic
plaques

Question : How biotechnology is defined by European Federation of

Biotechnology?
The European Federation of Biotechnology defines biotechnology as follows: "The integration of natural
sciences in order to achieve the applications of organisms, cells, parts there of and molecular analogues for
products and services."

Question : what is brewing?

Brewing is the production of beer by steeping a starch source (commonly cereal grains, the most popular of
which is barley) in water and fermenting the resulting sweet liquid with yeast.

Question : Define Electrolytes and its functions.

Electrolytes:Electrolytes are minerals that carry an electric charge when they are dissolved in a liquid such as
blood. (OR) Electrolytes are molecules that release ions in water. Common electrolytes include calcium,
chloride, magnesium, phosphorous, potassium and sodium.Function of electrolyte:Maintaining fluid
balance Facilitating enzyme reactions Transmitting neuromuscular reactionsRegulate nerve and muscle
function Effect the amount of water in body and PH of bloodRegulate Acid base balanceRegulate water
balance.

Question : Write note on buffer system.

The chemical buffer systems in body fluids include;1. Bicarbonate buffer system2. Phosphate buffer
system3. Protein buffer system1. Bicarbonate buffer system:Bicarbonate buffer system produces carbonic
acid (H2CO3) and sodium bicarbonate (NaHCO3) to minimize H+ increase, mainly in the bloodCarbonic acid
(H2CO3) converts a strong base into a weak base.NaOH + H2CO3 NaHCO3 + H2OBicarbonate ion (HCO3)
converts a strong acid into a weak acid.HCI + NaHCO3 H2CO3 + NaCI2. Phosphate buffer systemThe
Phosphate buffer system operates in the internal fluid of all cells. This buffer system consists of dihydrogen
phosphate ions (H2PO4) as hydrogen ion donor (acid) and hydrogen phosphate ions (HPO4) as hydrogen
acceptor (base).If additional hydrogen ions enter the cellular fluid, they are consumed in the reaction with
hydrogen phosphate ions (HPO4)If additional OH enter the cellular fluid, the react with dihydrogen phosphate
ions (H2PO4) and maintain the PH.3. Protein buffer system:The protein buffer system is the most important
and widely operating buffer in the body fluid.Protein molecule possess both acidic (carboxylic group) and
basic (amino group) groups.The carboxylic acid group of protein release H+, and the amino group accept H+,
mainly inside body cells and in blood plasma.An example of a protein buffer is is hemoglobin

Question : What are Amino Acids?

Amino Acids:Amino acids are the basic structural constituents of naturally occurring proteins. They all consists
of amino group (NH+3), a carboxylate group (COO-), a hydrogen atom and a There are 20 standard amino
acid.These twenty different amino acids, join together with different combination to from different kinds of
protein.

Question : What are carbohydrates?

The carbohydrates are the polyhydroxy aldehydes or ketones or their complex substances which on
hydrolysis give polyhydroxy aldehydes and ketones.

Question : What is scope of Biochemistry?

It is used in clinical diagnosis, manufacture of various biological products, treatment of diseases, in nutrition,
agriculture. Biochemistry in general deals with body substance like enzymes, carbohydrates, amino acids, fats,
proteins, hormones, DNA, RNA, pigments, etc

Question : what is chief source of carbohydrates?

cereals are the chief source of carbohydrates.

Definition & General Formula Of

Carbohydrates
Question : How carbohydrates provide energy?
The simple sugars are absorbed directly by the small intestine into blood stream. But the disaccharide and
polysaccharide do not absorb in blood directly. They are first converted into monosaccharide. This bond
breaking also provides energy. Then the monosaccharides are absorbed by blood.

Question : what is biochemistry?

Biochemistry is the study of the chemical substances and vital processes occurring in living organisms. The
study of the chemistry behind biological processes and the synthesis of biologically active molecules are
examples of biochemistry.

Question : Define carbohydrates.

CARBOHYDRATES:Carbohydrates are aldehyde or ketone compounds with multiple (two or more) hydroxyl
(OH) groups. ORPolyhydroxylated compounds with at least three carbon atoms, with active carbonyl groups
which may either be aldehydeer or ketone, are called carbohydrates.Carbohydrates composed of C,H,O. Some
carbohydrates also contain N,P,or S.They are the most abundant biomolecule on earth, however they from
only 1% of the human body mass.Carbohydrates are hydrated carbons, because hydrogen and Oxygen in
Carbohydrates were found to be present in the same proportion as in water. (2:1).(E.g. Glucose C6H12O6 or
[C6(H2O)6].But many carbohydrates contain H and O not in same proportion as in water. E.g. deoxyribose
whose molecular formula is C5H10O4.

Question : What are the functions of carbohydrates in human

body?
Carbohydrates perform following major functions in the body:Construction of body organsAssist in body
absorption of calciumHelps in lowering of glucose levelsKeep water-mineral balanceProvides nutrients to GIT
friendly bacteria that help in digestion

Question : How many functional groups are present in the

carbohydrates?
There are two functional groups in carbohydrates that are:ketone group. ( the sugars containing ketone
group are called ketose sugars)aldehyde group ( the sugars containing aldehyde group is called aldose sugar)

Question : How carbohydrates are naturally produced?

The carbohydrates are prepared by the plants by the process of photosynthesis. The photosynthesis involves
the following reaction. CO2 + H2O ?????? C6H12O6 + O2

Question : What is gluconeogenesis?

Gluconeogenesis (abbreviated GNG) is a metabolic pathway that results in the generation of glucose from
non-carbohydrate carbon substrates such as lactate, glycerol, and glucogenic amino acids.
Question : What is function of biochemistry in medicine?
It describes their origin, formation, function, deficiency symptoms, etc. It tries to explain life regarding
biochemical reactions.Based on the symptoms described by the patient, the physician can get a clue on the
biochemical change and the associated disorder. For example, if a patient complains about stiffness in small
joints, then the physician may predict it to be gout and get confirmed by evaluating uric acid levels in the
blood. As uric acid accumulation in blood results in gout. ·

Question : Define Aldehydes and Ketone.

Aldehydes:Compounds in which the carbon of carbonyl group is bonded to Hydrogen (H) and carbon/alkyl
group (R) are called aldehydes.Carbohydrates containing aldehyde group on first carbon of its structure are
called aldose or aldose sugar. E.g: Glycerose (glyceraldehyde), Glucose, RiboseKetones:Compounds in which
the carbon of carbonyl group is bonded to two other carbons or alkyl group (R) are called
ketonesCarbohydrates containing ketone group on second carbon of its structure are called ketose or keto
sugar. E.g; Dihydroxyacetone, Fructose, Ribulose

Question : What are the characteristics of monosaccharides?

They are sweet in taste.They cannot be further hydrolyzed.They are generally soluble in water.

Question : What are the normal fasting and random human blood
glucose levels?
Fasting glucose levels: 80 - 100 mg/dlRandom glucose levels: 100- 120 mg/dl

Question : Give some examples of ketose sugar.

FructoseErythruloseribuloseSedoheptulose

Question : What is the composition of lactose?

Lactose is made up of two monosaccharide units i.e; glucose and galactose. Lactose is also called milk sugar.
Question : What is metabolism?
the chemical processes that occur within a living organism in order to maintain life. it consists of two types of
reactions i.e; anabolism and catabolism

Question : What are the functions of carbohydrates in human

body?
Carbohydrates perform following major functions in the body:Construction of body organsAssist in body
absorption of calciumHelps in lowering of glucose levelsKeep water-mineral balanceProvides nutrients to GIT
friendly bacteria that help in digestion

Question : How many functional groups are present in the

carbohydrates?
There are two functional groups in carbohydrates that are:ketone group. ( the sugars containing ketone
group are called ketose sugars)aldehyde group ( the sugars containing aldehyde group is called aldose sugar)

Question : How carbohydrates are naturally produced?

The carbohydrates are prepared by the plants by the process of photosynthesis. The photosynthesis involves
the following reaction. CO2 + H2O ?????? C6H12O6 + O2

Question : What is gluconeogenesis?

Gluconeogenesis (abbreviated GNG) is a metabolic pathway that results in the generation of glucose from
non-carbohydrate carbon substrates such as lactate, glycerol, and glucogenic amino acids.

Question : What is function of biochemistry in medicine?

It describes their origin, formation, function, deficiency symptoms, etc. It tries to explain life regarding
biochemical reactions.Based on the symptoms described by the patient, the physician can get a clue on the
biochemical change and the associated disorder. For example, if a patient complains about stiffness in small
joints, then the physician may predict it to be gout and get confirmed by evaluating uric acid levels in the
blood. As uric acid accumulation in blood results in gout. ·
Question : Define Aldehydes and Ketone.
Aldehydes:Compounds in which the carbon of carbonyl group is bonded to Hydrogen (H) and carbon/alkyl
group (R) are called aldehydes.Carbohydrates containing aldehyde group on first carbon of its structure are
called aldose or aldose sugar. E.g: Glycerose (glyceraldehyde), Glucose, RiboseKetones:Compounds in which
the carbon of carbonyl group is bonded to two other carbons or alkyl group (R) are called
ketonesCarbohydrates containing ketone group on second carbon of its structure are called ketose or keto
sugar. E.g; Dihydroxyacetone, Fructose, Ribulose

Question : What are the characteristics of monosaccharides?

They are sweet in taste.They cannot be further hydrolyzed.They are generally soluble in water.

Question : What are the normal fasting and random human blood
glucose levels?
Fasting glucose levels: 80 - 100 mg/dlRandom glucose levels: 100- 120 mg/dl

Question : Give some examples of ketose sugar.

FructoseErythruloseribuloseSedoheptulose

Question : What is the composition of lactose?

Lactose is made up of two monosaccharide units i.e; glucose and galactose. Lactose is also called milk sugar.

Question : What is metabolism?

the chemical processes that occur within a living organism in order to maintain life. it consists of two types of
reactions i.e; anabolism and catabolism

Question : How carbohydrates are classified?

Carbohydrates are classified as follows:MonosaccharidesDisaccharidesOligosaccharidesPolysaccharides

Question : What are heterogeneous disaccharides?

The disaccharides that yield all different monosaccharides upon hydrolysis are known as heterogeneous
disaccharides. For example; sucrose

Question : What is catabolism?

The metabolic reactions that break down the large molecules into smaller ones releasing the energy is called
catabolism.

Question : What is anabolism?

the synthesis of complex molecules in living organisms from simpler ones together with the storage of energy
is called anabolism. It is also called constructive metabolism.

Question : Give some examples of aldose sugars.

GlucoseErythroseRiboseGlucoheptose

Question : How many types of molecules are present in starch?

There are two types of molecules in starch. these are:AmyloseAmylopectin

Question : What is the exception to general formula of

Carbohydrates?
Exception: 1) That do not follow general formula but are sugars There are some such carbohydrates which
contain nitrogen, phosphorous or sulphur also in addition to carbon. Rhamnose has a Formula C6H12O5.
Exception: 2) Follow general formula but are not sugars Also all the compounds having formula
Cn(H2O) n may not be carbohydrates formic, acetic and lactic acids are some examples of such compounds.

Question : How monosaccharides are classified?

Monosaccharides are classified on the basis of functional group as follows:AldoseKetose

Question : What is the composition of maltose?

It is composed of Two monosaccharide units i.e; glucose + glucose. It is also fruit sugar.
Question : What do you know by fructose?
Fructose is a monsaccharide. 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.

Question : What are homogeneous disaccharides?

If all sugar molecules or monosaccharides are same in a disaccharide then they are homogeneous
disaccharides. For example; Maltose

Question : What are disaccharides?

Disaccharides are the carbohydrates having two sugar molecules,.They give two monosaccharide units on
hydrolysis. Disaccharides occur naturally. They are less sweet than monosaccharides. The two
monosaccharide units are joined thogether with glycosidic linkages. Disaccharides are white crystalline solids.
They are soluble in (H2O) water .Their molecular mass greater than monosaccharide.

Question : How many Functional Groups are present in

Carbohydrates?
Functional Groups of Carbohydrates:Functional Groups:It is a specific group of atoms or bonds which are part
of a larger hydrocarbon chain. (Provide a specific chemical behaviour).Carbonyl group:A carbon atom double
bonded to an oxygen atom is called carbonyl group. For carbohydrates, the functional group is the carbonyl
group which may be either aldehyde or ketone.

Question : Give some examples of polysaccharides.

CelluloseStarchGlycogenMucilageHemi cellulose

Question : What is the difference between homopolysaccharides &

heteropolysaccharides?
The polysaccharides that yield one type of monosaccharide molecules upon hydrolysis are called
homopolysaccharides. e.g; Starch, Glycogen The polysaccharides that yield different types of
monosaccharide molecules upon hydrolysis are called hetropolysaccharides. e.g; Mucilage, Hemicellulose
Question : What is sucrose?
Sucrose is common table sugar. It is a disaccharide, a molecule composed of two monosaccharides: glucose
and fructose. Sucrose is produced naturally in plants, from which table sugar is refined. It has the formula
C12H22O11.

Question : What are the properties of lipids?

They are insoluble in water (hydrophobic) but soluble in non-polar solvents (ether, chloroform,
benzene). Their primary building blocks are fatty acids, glycerol, sphingosine and sterols.\ In most cases, they
can be utilized by the living organisms. Most common lipid is fat in animals & plants Lipids are used to store
energy because of higher proportion of C-H bonds and very low proportion of oxygen , oxygen store double
the amount of energy as compared to the same amount of any carbohydrates

Question : What are the saturated fatty acids?

They do not contain double bond. “Animal fat are usually saturated” Fats containing saturated fatty acids are
solids at room temperature Example Butyric acid C3H7COOH

Question : What is sebum wax?

Sebum is a secretion of human skin having waxes. It helps skin to be moist and flexible.

Question : What do you know about 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

Question : Write the classification of lipids of lipids.`

Classification of lipids:Lipids are classified into three groups.1. Simple lipids 2. Compound Lipids3. Derived
lipids1. Simple lipids: These are ester of fatty acids with alcohols /glycerol. Simple lipids include;a. Fats: Fats
are ester of fatty acids with glycerol b. Waxes: these are ester of fatty acids with alcohol other than glycerol.
OR these are long chain of fatty acids bound to long chain of alcohol.2. Compound/Complex lipids: These are
ester of fatty acid with alcohol containing additional groups such as phosphate, nitrogenous bases. These
lipids include;a. Phospholipids: In addition to fatty acid and alcohol they contain phosphoric acid as an
additional group. They are further divided into two lipids.i. Glycerophospholipids: In which the alcohol is
glycerolii. Spingophospholipids : In which the alcohol is sphingosineb. Glycolipids or glycosphingolipids: In
addition to fatty acid and alcohol (sphingosine) these lipids contain carbohydrates as an additional
group.c. Lipoproteins: In addition to fatty acid and alcohol these lipids contain protein as an additional
group.d. Sulfolipids: In addition to fatty acid and alcohol these lipids conatin sulfate group as a/n additional
group.3. Derived lipids: These are the hydrolytic product of simple and compound lipids. They are alcohols,
sterols, vitamin D,E,K and carotenoids.

Question : What are waxes?

These are esters of fatty acids with long chain monohydric alcohols. RCOOH + ROH ―→ RCOOR +
H2O

Question : Define Lipids and write its characteristics.

Lipids are organic substance that occurs in living organisms and are soluble in organic solvents and insoluble
in aqueous solvents. ORLipids are the substances having the following characteristics.They are hydrophobic in
nature. i.e insoluble in water Soluble in organic solvents or non-polar solvents or fat solvents like acetone,
benzene, other, chloroform.Esters of long chain fatty acids and alcohols They primary blocks are fatty acids,
glycerol, sphingosin and sterolsThey usually have more C-H bonds and less O as compared to
carbohydratesFatty acid esters (FAEs) are a type of ester that result from the combination of a fatty acid with
an alcohol. When the alcohol component is glycerol, the fatty acid esters produced can be monoglycerides,
diglycerides , Dietary fats are chemically triglycerides.An ester is an organic compound where the hydrogen in
the compound's carboxyl group is alcohol. While carboxylic acid has the-COOH group, the hydrogen is
replaced by a hydrocarbon in an ester. The chemical formula of an ester takes the from RCO2R, where R is the
hydrocarbon parts of the carboxylic acid, and R is the alcohol. The term "ester" was coned by the German
chemist Leopold Gmelin in 1848. It is likely the term was a contraction of the German word essigather, which
means "acetic ether."Lipids in include:Fats (solid triglyceroids. E.g: ghee)Oils (liquid triglyceroids. E.g:
oils)SteroidsWaxes

Question : What are unsaturated fatty acids?

They contain one or more double bond in their formula. Plant fats are mostly unsaturated. Fats containing
unsaturated fatty acids are liquid at room temperature

Question : What do you know by cholesterols?

It is most abundant animal sterol. It occurs in animal tissues most abundant in the adrenal gland followed by
nervous system. Normal plasma level ranges from 150 to 220mg/dl. Some 140 grams of cholesterol may be
present in an adult human being. It also present in plasma membranes of tissue cells & in plasma
lipoproteins.

Question : To which organ the lipids provide the stability?

Body fat gives anatomical stability to organs like kidney. When a person loses weight rapidly, his kidney is
liable to become floating kidneys.

Question : In how many groups the complex lipids are divided?

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 sustituents. 4. Lipoproteins
These are complex of lipid with proteins.

Question : What are fast / Triglycerides and maxes?

Fats / Triglycerides:Fat are ester of fatty acids with acids with glycerol. It is also called triglycerides or
triglycerol. Waxes:Ester of fatty acids with high molecular weight alcohol.

Question : What are the different types of fatty acids?

There are two types of fatty acids. these include:Monounsaturated fatty acids i.e. Oleic
acid C18H33COOH Polyunsaturated fatty acids i.e. Archidonic acid C19H31COOH

Question : What are the waxes?

These are esters of fatty acids with long chain monohydric alcohols. RCOOH + ROH ―→ RCOOR +
H2O

Question : How triglycerides are formed?

glycerol and carboxylic acid molecules react together to form triglycerides. Glycerol+3Carboxylic acid -------
→Triglycerides+3CO2+3H2O
Question : What is the composition of phospholipids?
The phospholipids are composed of:Alcoholsfatty acidsphosphoric acidsthey also frequently contain N-
containing bases

Question : Define Fatty acids and types of lipids.

Fatty acids:Fatty acids are organic acids consists of hydrocarbon (C-H) chain with methyl group at one end and
acidic group (COOH) at the other end.Types of fatty acids:Fatty acids may be saturated or
unsaturated Saturated fatty acids:These fatty acids have no double bonds in their hydrocarbon chain.Can't
accommodate any more hydrogenSolid at room temperatureStored inamimals as fatsExamples: Butter, ghee,
palmatic acid, stearic acid, arachidic acidUn-saturated fatty acids:These fatty acid s have one or more double
bonds in their hydrocarbon chain Can accommodate more hydrogenExamples: palmitoleic acid, Olie acid

Question : Where are waxes found?

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.

Question : What are sterols?

A sub group of steroids is sterols which contain one or more –OH groups and no carbonyl and carboxyl
groups; their names end in -ol. Examples Some of natural compound belonging to steroids are cholesterol,
ergosterol, bile acids, male and female sex hormones and the hormones of adrenal cortex.

Question : Define Glycerol.

Glycerols:Glycerol is a three carbon compound and OH group is attached to each carbon.Glycerol is low
molecular weight alcohol.

Question : What are lipids?

The lipids are organic substances occurring in plant and animal tissues belong to a very heterogeneous group
of compounds related to fatty acids. Lipids include fats, oils, waxes, steroids

Question : How are the lipids classified?

lipids are classified as follows: I. Simple Lipids II. Compound Lipids III. Derived Lipids

Question : Write the functions of lipids:

Function of lipids:Good source of energy having high caloric value usually yield twice as much energy as that
of carbohydratesAct as electric insulator in nervous systemEssential for the absorption of fat soluble
substance like fat soluble vitamins A,D,E,K.Lipids are the integral part of cell membrane Act as a precursor of
some important biological compounds. E.g: cholesterol is the precursor for steroid hormones

Question : What do you know about albuminoids?

These are also called scleroproteins [sclero = hard] and occur only in animals; they do not occur in plants.
These proteins includes: Collagen Elastin Keratin

Question : What are 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.

Question : Name the amino acids with COOH GROUP.

The only example of this type is proline.

Question : What do you know about albumin?

Albumin is a protein made by the liver that keeps fluid from leaking out of blood vessels. It is the most
abundant protein in the human blood plasma. 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.

Question : Name the amino acids with Side chain containing

hydroxyl (-OH) group
serine and threonine.

Question : Name the amino acids with acidic side chains

These include glutamic acid and aspartic acid;

Question : Name the amino acids with non-polar aliphatic side

chains.
Glycine Alanine Valine Leucine Isoleucine

Question : What is the general formula of amino acid?

The amino acid contain two characteristic functional groups i.e; amino group and carboxylic group. all amino
acids contain an -R group that varies in different amino acids.

Question : Name the amino acids with aromatic side chains.

These include phenylalanine tyrosine and tryptophan

Question : Name the amino acids with side chains containing sulfur
(S) atom
cysteine and methionine.

Question : What is the function of Pantothenic acid.

It is a widely distributed vitamin; it forms a part of the of coemzyme A (abbreviated as CoA-SH or just CoA)
which takes of metabolic reactions.

Question : What is the Quaternary structure of proteins?

Quaternary structure is the arrangement of more than one protein molecule in a multi-subunit complex The
structure formed by aggregation of two or more polypeptide chain is called quaternary structure the
aggregation of such polypeptides chain form one functional macromolecule. Each poly peptide chain is called
subunit. e.g. Hemoglobin, Collagen etc..

Question : How does the proteins help in clotting of the blood?

They are involved in blood clotting through thrombin fibrinogen and other protein
factors. Fibrinogen comprises 7% of blood proteins; conversion of fibrinogen to insoluble fibrin is essential for
blood clotting.

Question : Give a brief introduction to prolamins.

Prolamins are a group of plant storage proteins having a high proline content and found on plant materials
mainly like in the seeds of cereal grains. These are soluble in 70 to 80% ethanol but are insoluble in water and
absolute alcohol. Examples are gliadin of wheat and zein of maize. These are rich in the amino acid proline
but deficient in lysine.

Question : Which amino acid is abundant in histones?

Histones are very strongly basic proteins as they are rich in arginine. In combination with deoxyribonucleic
acid (DNA) they form nucleoproteins (nucleohistones). The association of DNA and histones gives rise to
complexes called nucleosomes.

Question : Which amino acids are absent and which are abundant
in protamines?
The amino acids absent in protamines include:tyrosinetryptophanThe amino acid present in abundance in the
protamines is arginine.

Question : Name the amino acids with basic side chains

These include lysine, arginine and histidine

Question : What are the globulins?

hese 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.

Question : How does proteins take part in the homeostatic control

of the body?
The function of proteins in the homeostatic control is to control the volume of the circulating blood and that
of the interstitial fluids through plasma protein. Plasma proteins take part in blood coagulation and transport
of substances such as hormones drugs, metal like iron and copper.

Question : What are the compound or conjugated proteins?

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. Nucleoproteins. Phosphoprotien
Lipoproteins Carbohydrate - containing proteins Chromoproteins Metalloproteins

Question : Give some examples of globulin proteins.

Lactoglobulin Myosin in muscle Ovoglobulin Serum globulins

Question : What is the role of proteins in contractility of muscles?

Most proteins are involved in contractility e.g. dyne in cilia and flagella. Tubulin in spindle fibres. Actin and
myosin in muscles.

Question : Write down the functions of amino acids.

“Amino acids are building blocks of Proteins” . So all the functions which proteins perform are the function of
amino acidsi) A group of substances called enzymes which are biocatalyst of the body, “Enzymes are mainly
protein in nature. ii) Hormonal effect. Many of the hormones which regulate the chemicals and other process
or the body are also protein in nature. iii) They play role as: Hormone biosynthesis N2 metabolism Tolerance
of certain environmental stresses e.g. Proline stores under salt stress condition in plants

Question : What is the function of GABA?

It occurred in brain and other tissues it has an important physiological role as neurotransmitter.

Question : What are proteins?

Proteins are extremely complicated molecules and are the nitrogenous compounds made up of variable
number of amino acids joined to each other by a specific type of covalent bond called peptide bond or
peptide linkage.

Question : how proteins are classified on the basis of

physicochemical properties?
on the basis of physicochemical properties the proteins are classified into 3 groups:simple proteinscompound
or conjugated proteinsderived proteins

Question : What is the Function of Dihydroxyphenylalanine?

It is formed in tissues during the metabolism of phenylalanine and tyrosine. L- Dopa is being used in treating
Parkinsonism as in the brain it give rise to dopamine which is a neurotransmitter.

Question : What are the non standard amino acids?

The non-standard amino acids are those amino acids which, contrary to the standard amino acids already
described, do not take part in protein synthesis but many of them play important role in the body. There are
several hundreds of such amino acids, a few of which having important physiological functions are given
below. Citrulline Ornithine Argininosuccinic acid

Question : Name the different types of simple proteins?

The different types of the simple proteins include; Albumin Globulin Globin Prolamin Histones Protamines
Albuminoids

Question : How does proteins take part in the defense of the 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.

Question : What is the function of proteins as the structural

material?
Proteins are the structural material for the plant and animal. Protein form the major part of dry weight of
plant and animal protein are the major part of all the membrane system of cell. Proteins take an essential part
in the formation of protoplasm which is the essence of all forms of life.

Question : What are the different types of nucleic acids?

There are two types of nucleic acids:DNA ( Deoxyribonucleic acid)RNA ( Ribonucleic acid)

Question : What is Chargaffs law?

Chargaffs law states that:Total purines= Total pyrimidinesA is always equal to T and G is equal to C
Question : What are nucleic acids?
Nucleic acid are biopolymers or small biomolecules essential to all known forms of life. They are composed of
nucleotides which are monomers made of three components: a 5-carbon sugar, a phosphate group and a
nitrogenous base.

Question : What is difference between RNA and DNA?

Difference between RNA and DNA: RNA Pentose sugar is ribose In RNA nitrogenous bases are Adenine (A)
Guanine (G), Cytosine (C) and Uracil (U)Single strand structure Smaller in size DNA Pentose sugar is
deoxyriboseIn DNA nitrogenous bases are Adenine (A), Guanine (G), Cytosine (C) and Thiamanie (T).Double
strand structure Larger in size

Question : Where are nucleic acids are found?

Nucleic acids are found in every living cell as well in the viruses and has been found as an essential substance
of the genes and the apparatus by which the genes act.

Question : What are Different components of nucleic acids?

Nucleic acids are composed of nucleotide units or mononucleotides. Each nucleotide is composed of:A
nitrogenous baseSugar phosphoric acid complex

Question : What are the components of nucleic acids?

Both DNA and RNA are formed by joining together of a large number of nucleotide units or mononucleotides,
each of which is a nitrogenous base-sugar-phosphoric acid complex. In other words, nucleic acids are
polynucleotide.

Question : What is the physical appearance of nucleotides?

Nucleic acid molecules are usually unbranched, and may occur as linear and circular molecules. For example,
bacterial chromosomes, plasmids, mitochondrial DNA and chloroplast DNA are usually circular double-
stranded DNA molecules, while chromosomes of the eukaryotic nucleus are usually linear double-stranded
DNA molecules. Most RNA molecules are linear, single-stranded molecules.
Question : What units make unit nucleic acids?
Nucleic acids are formed by sequences of nucleotides.Nucleotides are composed of one molecule of sugar
(deoxyribose in DNA and ribose in RNA) bound to one molecule of phosphate and to one nitrogenous base
(adenine, uracil, cytosine or guanine, in RNA; and adenine, thymine, cytosine and guanine, in DNA).

Question : Define RNA (Ribonucleic acid) and types of RNA.

RNA (Ribonucleic acid):RNA is a single strand nucleic acid and is much more abundatn than DNAIn RNA the
pentose sugar is ribose and nitrogenous bases are Adenine (A), Guanine (G), Cytosine (C) and Uracil (U)Types
of RNA:1. Ribosomal RNA (rRNA): Ribosmal RNA is located in the cytoplasm of cell where ribosome are found.
It comprises 75% of the total RNA. It is mainly responsible for the synthesis of protein.2. Messenger RNA
(mRNA): Messenger RNA carries genetic code or information for protein synthesis from DNA to the ribosmoe.
IT comprises 5-10% of the total RNA. 3. Transfer RNA (tRNA): Transfer RNA translates the genetic codes from
mRNA and brings amino acids to the ribosome for protein synthesis. Each amino acid is recognized by
transfer RNA. It comprises 10-15% of the total RNA.

Question : What is translation?

Translation is the synthesis of a protein from an mRNA template where the code in the mRNA is converted
into an amino acid sequence in a protein.

Question : What is transcription?

Transcription is the synthesis of RNA from a DNA template where the code in the DNA is converted into a
complementary RNA code.

Question : What is the difference between DNA and RNA from the
point of view of the nitrogenous bases that are present in their
nucleotides?
In DNA, nucleotides can be made up of adenine (A), thymine (T), cytosine (C) or guanine (G). In RNA,
nucleotides can also contain adenine (A), cytosine (C) or guanine (G); however, instead of thymine (T), they
contain uracil (U).
Question : According to the Watson-Crick model, how many
polynucleotide chains does a DNA molecule have?
A DNA molecule is formed by two polynucleotide chains bound in antiparallel mode (5’-3’ to 3’-5’) and which
form a helix structure.

Question : Which type of chemical bond maintains the pairing of

each chain in the DNA molecule?
To form the DNA molecule, purine bases bind to pyrimidine bases via intermolecular bonds called hydrogen
bonds. Hydrogen bonds occur when there is a hydrogen atom near one of the following electronegative
elements: fluorine, oxygen or nitrogen.In such conditions, hydrogen appears to have lost electrons to those
elements and a very strong polarization is created. The highly positive hydrogen atom attracts pairs of
electrons from other molecules, making a hydrogen bond.

Question : Name the pyrimidine bases.

CytosineUracilThymine

Question : What is the molecular shape of RNA?

RNA is the single stranded structure that may be coiled on itself and in certain cases has double helix parts.
Rarely double stranded RNA have been found even in humans.

Question : What are different types of RNA?

There are 3 types of RNAmessenger RNA (mRNA)Transfer RNA (tRNA)Ribosomal RNA (rRNA)

Question : What are the components of RNA nucleotide?

The components of RNA nucleotide are:a nitrogenous base which may be either a purine (adenine or guanine)
or a pyrimidine (cytosine or uracil)Ribose which is actually D-ribosePhosphoric acid

Question : What is the function of mRNA?

Messenger RNA (mRNA) carries the genetic information copied from DNA in the form of a series of three-base
code ?words,? each of which specifies a particular amino acid.

Question : Name the heterocyclic bases.

The heterocyclic bases include:pyrimidines ( they include Uracil, Cytosine and Thyamine)purines ( they include
Adenine and Guanine)

Question : What is the location of DNA in cell?

The DNA is found in the nucleus, some is found in cytoplasm. it is also found in the mitochondria.

Question : What is the double helix of DNA?

Double helix of DNA is the model of DNA shape proposed by Watson & Crick in 1953. it proposes that DNA is
composed of two anti-parallel strands of polydeoxyribonucleotoide chains that are wound on each other.
These strands are joined by nitrogenous bases i.e; adenine joins thymine and guanine joins to cytosine.

Question : What are two major functions of DNA?

to store genetic informationreplication

Question : What is the biological role of DNA?

DNA is the ultimate carrier of heredity in all eukaryotes and even most prokaryotes except certain viruses and
phages. Genes are composed f DNA in which the genetic information is contained in the form of codes. The
double helical structure of DNA.explains many of the properties of DNA. DNA has two important
properties; to store genetic information and replicate, i.e. to synthesize double-stranded DNA exactly similar
to the DNA originally present and to produce mRNA (transcription) which will dictate the synthesis of proteins

Question : Write a note on the structure of Nucleic acids.

Nucleic acids:Nucleic acids for the first time was isolated by friedrich in 1869 from the nuclei of pus cells. He
called it nuclein and later on it was called nucleic acid because of acidic properties.Nucleic acids are essential
biological molecules that consists of nucleotidesThey are composed of carbon, hydrogen, oxygen, nitrogen
and phosphorus The are located in the nuclei of cellThey are hereditary determinants of living
organismsNucleotides:Nucleotides are the building block of all nucleic acids. Each nucleotide has three
components;1. Phosphate r group1. 5-Carbon sugar (Pentose)3. Nitrogenous base1. Phosphate group:It is a
chemical derivative of phosphoric acid. (OR) it is an ester of phosphoric acid2.5-Carbon sugar (Pentose):5-
Carbon sugar (Pentose) may be Ribose or Deoxyribose. If it is ribose then the polymer of nucleotide RNA
and Nucleoside:It consist of Nitrogen base and 5-Carbon sugar (Pentose)There is no phosphate group. When
the phosphate group is added to nucleoside then it is Called nucleotide.3. Nitrogenous base:Nitrogenous base
include purines and pyrimidines Purines include adenine (A) and Guanine (g)Pyrimidine includes cytosine (C),
uracil (U) and thymine (T).

Question : Define DNA (Deoxyribo nucleic acid) and its functions.

DNA (Deoxyribo nucleic acid):DNA is a double strand and large nucleic acidIn DNA the pentose sugar is
deoxyribose and nitrogenous bases are Adenine (R), Guanine (G), Cytosine (C) and Thiamine (T).Function of
DNA:Permanent storage place for genetic informationLong-term storage of information in the cellPlay
important role in term of heredityIt stores all the genetic information and transfer to the next
generationControls the synthesis of RNAThe sequence of nitrogenous bases in DNA determine the protein
development in new cellsDNA holds instructions for an orgnisms development and reproduction Controls all
functions of the cells like regulation of protein, ribosmoes and RNAControl the response to external agents.

Question : What is the historical origin of nucleic acid?

The name “nucleic” derives from the fact that they were discovered (by the Swiss biochemist Friedrich
Miescher, in 1869) within the cell nucleus.

Question : What are hormones?

These are chemical substances that are secreted into the body fluids by one cell or the group of cells and have
the physiological control effect on the other cells of the body.

Question : What are the symptoms of hormonal imbalance?

symptoms of hormonal imbalances women include:Osteoporosis ( weak brittle bones)Hot flashes and night
sweatsindigestionConstipation and diarrheaacne

Question : What is the role of estrogen?

Estrogens are hormones that are important for sexual and reproductive development, mainly in women. They
are also referred to as female sex hormones. The term "estrogen" refers to all of the chemically similar
hormones in this group.

Question : Write any 4 functions of the hormones?

Play a key role in growth and developmenttransport substances through the cell membranecontributes to the
basic processes of reproductionRegulate the metabolism and energy balance in the body

Question : What is the effect of growth hormone on the inorganic

metabolism?
GH increases the retention of phosphorus and calcium in the body fluids by increasing the absorption from
GIT and renal tubules.It also causes the retention of sodium, potassium, chloride and ,magnesium.

Question : What is gluconeogenesis?

Gluconeogenesis (GNG) is a metabolic pathway that results in the generation of glucose from certain non-
carbohydrate carbon substrates.

Question : Why hormones are so important in the body?

Hormones, in their most basic sense, are chemical messengers. Hormones are released from specific organs
or glands in the body and travel through the blood stream to send messages to other cells. All of the cells
in our bodies have specifichormone receptors.

Question : Define endocrinology.

This is the science concerned with the structure and functions of the endocrine glands and the diagnosis and
treatment of the disorders of the endocrine system.

Question : What are the stimuli for milk ejection in lactating

mothers?
sucking of nipples of the breast by the babyHandling of the breasts by the babyCrying of the baby for
feedingSight or sound of baby.

Question : What are the effects of estrogen on external genitalia?

increases the size of the clitoris and labia minoraincreases the deposition of fat on the mons pubis and labia
majora
Question : How many types of hormones are there?
There are two types of hormones, these are:Local Hormones: These have specific local effects on the body.
e.g; Acetyl choline, secretin and Cholecystokinin.General Hormones: These affect body cells far away from
their points of secretion. A few general hormones affect all the cells of the body, such as growth hormone and
thyroid hormone. On the other hand, some hormones affect only on target cells because they have specific
receptors for the hormone. e.g. ACTH, estrogen, and progesterone.

Question : What are Harmones? And what do they do?

Hormones are special chemical messengers in the body that are created in the endocrine glands. These
messengers control most major bodily functions, from simple basic needs like hunger to complex systems like
reproduction, and even the emotions and mood. Understanding the major hormones and what they do will
help patients take control of their health.

Question : What is the role of hormones in the body?

Hormones are the body's little messengers, which get produced in one part of the body, such as the thyroid,
adrenal or pituitary gland, pass into the bloodstream or other body fluid and go to distant organs and tissues
where they act to modify structures and functions.

Question : Give some examples of general hormones.

ACTH (Adrenocorticotropic Hormone)progestroneestrogen

Question : What is human growth hormone?

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.

Question : Can low estrogen levels cause fatigue?

Low estrogen levels many times found in menopause, often result in insomnia and night sweats.
Diminished estrogen also causes irritability and mood swings in women Too little progesterone is also linked
to fatigue in women.This anxiety or depression brings with it fatigue.
Question : What is the clinical indication for the use of oxytocin?
the clinical indication for the use of the oxytocin is:to induce laborsfor the treatment of uterine haemorrhage

Question : How does oxytocin favor fertilization?

Oxytocin accelerates the transport of seminal fluid towards the Fallopian tubes favoring fertilization.

Question : What does progestin do to the female body?

One of progesterone's most important functions is its role in thickening the lining of the uterus each month.
The enriched endometrial lining is prepared to receive and nourish a fertilized egg. If a pregnancy
occurs, progesterone is produced in the placenta and levels remain elevated throughout the pregnancy.

Question : What is the action of insulin on carbohydrates?

it increases the utilization of glucose for glucoseit increases glycogen storage in cells.it increases the
conversion of glucose into fat to be stored adipose tissues.it increases the entry of glucose into the cells.

Question : Which organ formation is promoted by testosterone in

fetus?
it causes the development of the male sex organs including the penis, scortum prostate, seminal vesicle and
male genital duct.

Question : What is the effect of testosterone on body length?

If testosterone is secreted in excessive amounts it decreases the length of the body due to the early fusion of
the epiphyses.

Question : What are the effects of testosterone on the secondary

sex characteristics?
increased growth of body hairdecreased growth of hair on head ( Baldness)Thickening of skinbroadening of
shouldersAggressiveness of the behavior
Question : What is the effect of testosterone protein metabolism?
It increases protein synthesis and build up the musculaturecauses positive nitrogen balancedecreases blood

Question : name the different types of estrogen?

three naturally occurring estrogens include:17-beta-estradiolestroneestriol

Question : How does the vaginal pH becomes acidic?

The vaginal pH becomes more acidic due to the conversion of glycogen into lactic acid by bacteria.

Question : Why is estrogen used for cosmetic purposes?

Estrogen increases the vascularity of the skin and causes the softness and smoothness of the skin. this is why
estrogen is used in creams, soaps, and oils for cosmetic purposes.

Question : Which food have high content of estrogen?

Fruits: apricots, oranges, strawberries, peaches, many dried fruitsVegetables; yams, carrots, alfalfa sprouts,
ksle, celeryDark rye breadlegumesolives and olive oils

Question : what is progesterone?

Progestrone is an endogenous steroid hormone involved in menstrual cycle, pregnanacy and embryogenesis
in humans and other species.

Question : what are the after-effects of low progesterone level in

women?
Low progesterone in woman may cause:Depression Migraines headacheweight gain

Question : name the solutions in which enzymes are precipitated.

concentrated alcoholAmmonium sulphateTrichloro acetic acid
Question : How are enzymes classified?
enzymes are classified into following main 6
classes:OxidoreductasesTransferasesHydrolysesLyasesIsomerasesligases

Question : What is the cofactor?

Many enzymes require an additional small molecule, known as a cofactor to aid with catalytic activity. A
cofactor is a non-protein molecule that helps the enzyme to carry out chemical reactions. Cofactors can be
either inorganic molecules (metals) or small organic molecules (coenzymes).

Question : What are enzymes?

Enzymes are the catalysts of biological system that are produced by the living cell which are capable of
catalyzing the biological reaction between certain reactants to yield specific product.

Question : How will you define catalyst?

Catalyst is a chemical which is used to boost up chemical reaction but it is not utilized itself in the chemical
reaction.

Question : What is the irreversible inhibitor of the enzymes?

An irreversible inhibitor will bind to an enzyme that no other enzyme-substrate complexes can form. It will
bind to the enzyme using a covalent bond at the active site which therefore makes the enzyme denatured.

Question : Define Enzymes

ENZYMES:Enzymes are biological molecules produce by living organisms that catalyze chemical
reactions.Enzymes are biological catalysts that speed up the rate of the biochemical reaction.Enzymes are
protein in nature. Most enzymes are three dimensional globular proteins having tertiary and quaternary
structure.

Question : Define Catalysts.

Catalysts:Catalyst is an agent that increase the velocity of a reaction without appearing in the final product. It
accelerate the rate of reaction without undergoing any permananent change. Eg. Platinium, zinc, vanadium

Question : Write the characteristics of enzymes.

Characteristics of enzymes:Enzymes speed up the reaction by lowering the activation energy of the
reaction.Their presence does not effect the nature and properties of end product.They are highly specific in
their action that is each enzyme can catalyze one kind of substrate.Small amount of enzymes can accelerate
chemical reactions.Enzymes are sensitive to change in pH, temperature and substrate concentration.

Question : Write note on nomenclature of enzyme.

The nomenclature of enzymes is derived form their substrates or the catalyzed chemical reactions, and "ase"
is usually added as a suffix. e.g.Lipase, Hydrolyzing the Fats, Lip for lipids (Fats) and ase is suffixCellulase;
Hydrolyzing the Cellulose. Cellul for cellulose and ase is suffixOxidase: catalyze oxidation reaction, Oxid for
oxidation reaction and ase is suffix Hydrolases: Catalyze hydrolysis reaction. Hydrola for hydrolysis reaction
and ase is suffixSome enzymes ware named before a systematic way of naming enzyme was formed.
Example: pepsin, trypsin and rennin.

Question : What is trypsin?

Trypsin is an enzyme that acts at the pH of 8.57. It is secreted by pancreas and is very important for the
digestion of the food.

Question : What are different types of transferases?

TransaminasesTransmethylasesTransacylasesTranspeptidasesPhosphotransferases ( Kinases)

Question : How enzymes are used in food industry?

Cheese manufacturing can be used as the sweetnerin meat tenderizingin alcoholic beverages

Question : How enzymes play their role in digestion?

Enzymes play an important role in digestion. it promotes digestion by conversion of large complex and non
diffusible molecules into smaller, simple and diffusible molecules. e.g; Amylase, trypsin and lipase
Question : Name any 4 enzymes of the digestive tract.
AmylaseLipaseTrypsinPepsin

Question : Name the enzymes that can be used in meat tenderizing.

The enzymes that can be used in meat tenderizing are:PepsinPapainTrypsin

Question : Write down the general reaction between the enzyme

and the substrate.
The general reaction between the enzyme and substrate is as follows:E +S → ES → E
P → E+P

Question : What is the Mechanism of enzyme reaction?

Mechanism of enzyme reaction:The enzyme molecule (E) first combine with a substrate (S) to form an
enzyme-substrate complex (ES) which further dissociate the product and enzyme.Enzyme once dissociated is
fee to combine with another molecule of substrate and product in similar way.

Question : What are the main Functions of Enzymes?

Function of Enzymes:Enzymes plays a vital role in our daily life. they perform following important
functions.Digestion; Enzymes play important role in digestion for the conversion of large complex and non
diffusible molecules into smaller, simpler and diifusible molecules. E.g: Trypsin, Lipase and AmylaseCheese
making; used in manufacture of cheeseSweetener; some enzymes are used as sweetener. E.g; Glycosidase
enzyme convert Sucrose into glucose and fructoseAs drugs; some enzymes are used as drugs if there isany
disturbance in the digestive system.Curing of dieases like for heart problems lactate dehydrogenase, liver
problem kinases are usedManufacture of alcoholic beveragesTenderization of meat; techniques used for
breaking down collagens in meant to make it more palatable.Decrease in activation energy As a
detergentBlood Clotting.

Question : What is trypsin?

Trypsin is an enzyme that acts at the pH of 8.57. It is secreted by pancreas and is very important for the
digestion of the food.
Question : What are different types of transferases?
TransaminasesTransmethylasesTransacylasesTranspeptidasesPhosphotransferases ( Kinases)

Question : How enzymes are used in food industry?

Cheese manufacturing can be used as the sweetnerin meat tenderizingin alcoholic beverages

Question : How enzymes play their role in digestion?

Enzymes play an important role in digestion. it promotes digestion by conversion of large complex and non
diffusible molecules into smaller, simple and diffusible molecules. e.g; Amylase, trypsin and lipase

Question : Name any 4 enzymes of the digestive tract.

AmylaseLipaseTrypsinPepsin

Question : Name the enzymes that can be used in meat tenderizing.

The enzymes that can be used in meat tenderizing are:PepsinPapainTrypsin

Question : Write down the general reaction between the enzyme

and the substrate.
The general reaction between the enzyme and substrate is as follows:E +S → ES → E
P → E+P

Question : What is the Mechanism of enzyme reaction?

Mechanism of enzyme reaction:The enzyme molecule (E) first combine with a substrate (S) to form an
enzyme-substrate complex (ES) which further dissociate the product and enzyme.Enzyme once dissociated is
fee to combine with another molecule of substrate and product in similar way.
Question : What are the main Functions of Enzymes?
Function of Enzymes:Enzymes plays a vital role in our daily life. they perform following important
functions.Digestion; Enzymes play important role in digestion for the conversion of large complex and non
diffusible molecules into smaller, simpler and diifusible molecules. E.g: Trypsin, Lipase and AmylaseCheese
making; used in manufacture of cheeseSweetener; some enzymes are used as sweetener. E.g; Glycosidase
enzyme convert Sucrose into glucose and fructoseAs drugs; some enzymes are used as drugs if there isany
disturbance in the digestive system.Curing of dieases like for heart problems lactate dehydrogenase, liver
problem kinases are usedManufacture of alcoholic beveragesTenderization of meat; techniques used for
breaking down collagens in meant to make it more palatable.Decrease in activation energy As a
detergentBlood Clotting.

Question : What is effect of temperature on enzyme activity?

As the temperature increases, so does the rate of reaction. But very hightemperatures denature enzymes.
The enzyme activity gradually increases with temperature up to around 37?C, or body temperature.

Question : What is optimum pH?

The pH at which the enzyme catalyzes the reaction at its ,maximum rate is called optimum pH. e.g; the
optimum pH for pepsin is 1-2 and that for trypsin is 8.0-9.0

Question : How DNA polymerase is obtained?

T. aquaticus is a bacterium that lives in hot springs and hydrothermal vents, DNA polymerase was first
isolated from this bacterium and can withstand temperatures upto 90 C.

Question : What are ligases?

The enzymes catalyze condensation reaction joining two molecules by forming C-O, C-S, C-N, and C-C bonds
along with energy releasing hydrolysis or cleavage of high energy phosphate. e.g; ATP, GTP

Question : What is the function of buffer in the body?

The function of a buffer is to prevent rapid changes in the pH of a body fluid by changing strong acids and
bases into weak acids and bases.The most important buffer system of the body consists of a weak acid and
the salt of that acid, which functions as a weak base.
Question : What is Biotechnology and Genetic engineering?
Biotechnology:Biotechnology is a field of life science that deals with the study of living organisms and
biological systems to create modified or new organisms or useful products.Genetic engineering:Genetic
engineering, also called genetic modification or genetic manipulation, is the direct manipulation of an
organism's genes using biotechnology. 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.Genetic engineering is a major component of biotechnology is genetic engineering. Biotechnology
would not be possible without genetic engineering. In this process manipulates cells genetic information using
laboratory techniques in order to change of living organisms.

Question : Define Body Fluids.

Body FluidsA typical adult body contains about 40 L of body fluids. Fluids occur in body compartments
(intracellular and extracellular compartments) and the movement of water and electrolytes between these
compartments is regulated.The average adult male is 63% water by weight while female is 52% water by
weight.Intracellular fluid (ICF):It the fluid which is present inside the cells. 25 L of body fluids (or 63%) are
intracellular fluid.Intracellular fluid has high concentrations of potassium, phosphate, and magnesium ions,
and lesser amounts of sodium, chloride, and bicarbonate ions.Extracellular fluid (ECF):The body fluids are
located outside of body cells are called extracellular fluid (ECF). Extracellular fluids have high concentrations of
sodium, chloride, and bicarbonate ions, and lesser amounts of potassium, calcium, magnesium, phosphate,
and sulfate ions.15 L(or 37%) of the body fluids are extracellular fluids.80% of ECF is interstitial fluid (which
includes lymph, synovial fluid, cerebrospinal fluid, GI tract fluids, and fluids in the eyes and ears).20% of ECF is
blood plasma.

Question : Write a note on Electrolytes balance.

Electrolytes balance:Electrolyte balance or salt balance is necessary to control fluid movements within the
body fluid compartments (intracellular and extracellular compartments).Electrolytes maintain normal fluid
levels in the fluid because the amount of fluid in a compartment contains depends on the amount (
concentration ) of electrolytes in it.If the electrolyte concentration is high, fluid moves into that compartment (
a process called osmosis).If the electrolyte concentration is low, fluid moves out of that compartment.To
adjust fluid levels, the body can actively move electrolytes in or out of cells. Thus, having electrolyte s in the
right concentrations (called electrolyte balance) is important in maintaining fluid balance among the
compartments.Sodium (Na) is the most important electrolyte in maintaining electrolyte balance.The kidneys
maintain electrolyte concentrations by filtering electrolytes and water from blood, returning some to the
blood, and excreting any excess into the urine. Thus, the kidneys maintain a balance between daily
consumption and excretion of electrolytes and water.If the balance of electrolytes is disturbed, disorders may
develop like dehydration, over hydration, heart , kidney and liver disorders.
Question : What is the importance of biotechnology?
Modern biotechnology has its roots in two areas of science namely molecular biology and microbiology.
Advancement in these two sciences has led to a better understanding of the biochemical processes and their
inter relation ship. This insight has been exploited for the development of biotechnology.

Question : What are the tools of genetic engineering?

The important tools of genetic engineering are listed below: ? Enzymes Vectors cDNA clone bank
or cDNA library gene bank or genomic library

Question : What is homestatis?

Homeostasis is self-regulating process by which biological systems tend to maintain stability while adjusting to
conditions that are optimal for survival.

Question : Which electrolytes are present in body fluids?

Electrolytes of body fluids include: SodiumChlorideSulphatepotassium nitrates

Question : what do you know about fermentation?

the chemical breakdown of a substance by bacteria, yeasts, or other microorganisms, typically involving
effervescence and the giving off of heat is called fermentation. it is the metabolic process that consumes
carbohydrates in the absence of oxygen.

Question : What is an alkali?

This is the combination of one of the alkaline e.g. sodium or potassium with a highly basic ion such as (OH-).

Question : What are the functions of electrolyes in human body?

The functions of electrolytes present in body fluid are given bellow: They are responsible for the maintenance
of most of the osmotic pressure of body fluids. They provide an optimum ionic balance for tissues to perform
their activities They participate in the regulation of the pH of body fluids They regulate the neuromuscular
irritability or excitability.
Question : Write a note on Acid Base balance.
Acid Base balance:Acids are electrolytes that release hydrogen ions (H+) when they are dissolved in
water. Bases are electrolytes are release hydroxide ions(OH-) when they are dissolved in water.The body acid
base balance is regulated by buffering system of the body.Acid-base balance is primarily regulated by the
concentration of H+ (or the pH level) in body fluids, especially ECF.Most H+ comes from metabolism--
glycolysis, oxidation of fatty acids and amino acids, and hydrolysis of proteins.Homeostasis of pH in body
fluids is regulated by acid-base buffer systems (primary control).Acid-base buffer systems are chemical
reactions that consist of a weak acid and a weak base, to prevent rapid, drastic changes in body fluid pH. one
of the most carefully regulated conc. in thy body is that of H+ ion.When acid (H+) is added to the blood, the pH
decreases. Then the increased acidity (decreased pH) is minimized by buffers which bind some of the added
H+.When acid is taken away, blood becomes more alkaline (pH increases). This change is minimized by
buffers, which release H+ and replace some of the acid that was lost.

Question : How Biotechnology is defined by British bio-

technologists?
The British bio-technologists define biotechnology as: "The application of biological organisms, systems, or
processes to the manufacturing and service industries".

Question : Which sciences are incorporated within biotechnology?

The sciences incorporated within biotechnology
include:MicrobiologyGeneticsPhysiologyPhysicsMathematicsChemistryIndustrial
TechnologyImmunologyBiochemistry

Question : What are the areas of interest of biotechnology?

The field of biotechnology can be divided into eight major areas. these are:Recombinant DNA technology
Hybridoma technology Enzyme and biocatalysts technologyPlant cell culture & Animal cell
cultureFermentation technologies Waste treatment and utilization Process engineering

Question : How US National Science Foundation defines

biotechnology?
US National Science Foundation has appropriately defined biotechnology as "Controlled use of biological
agents such as microorganisms or cellular components for the benefit of mankind".
Question : Write down the names of buffers systems of the body?
The Principal Buffer systems of body fluids are: Carbonic acid-bicarbonate system Phosphate systemHb-
oxyhemoglobin systemProtein system

Question : What is the basic idea of genetic engineering?

The DNA of one organism can express its characters in an other organism also. This is the main idea of
genetic engineering. Changes that occur in the DNA molecules (mutations) may lead to genetic disorders

Question : Which systems regulate the acid-base balance of the

body?
There are three systems which regulate acid-base balance in the body. Acid-base buffer systemRespiratory
system Renal system

Question : Which components in human body affect acid base

balance?
Components that affect acid-base balance
include: proteinchloridephosphorussodiumpotassiumcalciummagnesium

Question : Applications of Biotechnology:

Production of Biotechnology :Production of AntibioticsProduction of Hormone InsulinProduction of
VaccinesProduction of EnzymesGene TherapyImprovement in Fermentation ProductsDiagnosis of
DiseaseProduction of Transgenci Animals Development of Transgenic PlantsMolecular Farming for Healthcare
Products.

Question : Name some enzymes that are required for rDNA

technology.
Many enzymes are used as biological tools in rDNA technology. They include:Restriction endonucleases S1
nuclease DNA ligases Alkaline phosphatase Reverse transcriptaseDNA polymerase
Question : Which components in human body affect acid base
balance?
Components that affect acid-base balance
include: proteinchloridephosphorussodiumpotassiumcalciummagnesium

Question : Which techniques have been developed for the diagnosis

of diseases?
The techniques developed for the diagnosis of the diseases include:plasmid profile analysis genomic
fingerprinting multilocus enzyme electro-phoresisNucleic acid hybridization poly-merase chain reactionELISA

Question : What is an acid?

This may be defined as a substance that dissociates into one or more hydrogen ions (H+) and one or more
negative anions. It may also be defined as a proton donor or H+ donor.

Question : what is meant by term cloning?

Cloning is the process of producing genetically identical individuals of an organism either naturally or
artificially. In nature, many organisms produce clones through asexual reproduction.

Question : Write a note on structure of the Protein structures.

Protein structures:a) Primary structureb) Secondary structurec) Tertiary structured) Quaterrnary
structurea) Primary structureLinear sequence of amino acids in polypeptide chain Studied by sanger in 1951
in insulinb) Secondary strurctureThe folding of polypeptide chain into a specific coiled structure held together
by hydrogen bondc) Tertiary structure:When the secondary structure is arranged in three dimensional
structured) Quaternary structure:When protein molecule is made of more than one polypeptide chain
(subunit). E.g: hemoglobin, consists of two alpha and two beta subunits.Simple proteins:These protein on
hydrolysis yields only amino acids or their derivatives. E.g: albumine, globuline, protamine1. Conjugated or
compound proteins:Conjugated protein composed of simple proteins+non-protenious substance. The non-
proteinous substance. The non-protenious substance is called prosthetic group or cofactor. E.g:
nucleoprotein, phosphoprotein, liporotein.2. Derived proteins:These are not naturally occuring proteins &
derived from simple or conjugated protein. The are obtained from simple protein by action of enzymes.

Question : Write a note on functions of Proteins.

Protein function: Building block of body structure-keratinSource of energyEnzymes are protein in
natureTransportation - hemoglobin transport oxygenContractile function - actin, myosinHormones are
protein - insulinStorage Proteins - seeds and eggsDefensive proteins-antibodiesPlasma protein take part in
blood coagulation

Question : What are Proteins?

Proteins:Proteins are large complex organic molecules consists of carbon, hydrogen, oxygen, nitrogen,
sulphur and phosphorus. ORProteins are nitrogenous compounds made up of a variable number of amino
acids joined together by covalent bond called peptide bond or peptide linkage.Simply, proteins are the
polymers of amino acids.

Question : Write a note on the types of Amino Acids.

Types of Amino Acids:Standard amino acids:Amino acids which take part in protein synthesis. They are also
called primary amino acids and twenty in numbersNon-standard amino acids:Which don't take part in protein
synthesisEssential amino acids:Which are not produced by our body and must be taken in diet. E.g:
LeucineNon-essential amino acids:Which can be synthesized by our body. E.g: Alanine

Question : Define Peptide bond, Dipeptide and Polypeptide.

Peptide bond:The bond which links the amino acids together i.e. the bond b/w COOH group of one amino acid
and NH2 of another amino acid molecule.Dipeptide:Chain of amino acids with two peptide bonds means
three amino acid moleculesPolypetide:A molecule consists of three or more amino acids linked together by a
peptide bond is called polypeptide.

Word Meaning in English Meaning in Urdu

satiety state of fullness ‫سيری‬