808

MAHARASHTRA STATE BOARD OF TECHNICAL EDUCATION
(Autonomous)
(ISO/IEC - 27001 - 2005 Certified)
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SUMMER– 14 EXAMINATION
Subject Code: 0808 Model Answer Page No: 1/ 40
Important Instructions to examiners:

1) The answers should be examined by key words and not as word-to-word as given in the
model answer scheme.
2) The model answer and the answer written by candidate may vary but the examiner may try
to assess the understanding level of the candidate.
3) The language errors such as grammatical, spelling errors should not be given more
Importance (Not applicable for subject English and Communication Skills.
4) While assessing figures, examiner may give credit for principal components indicated in the
figure. The figures drawn by candidate and model answer may vary. The examiner may give
credit for any
equivalent figure drawn.
5) Credits may be given step wise for numerical problems. In some cases, the assumed constant
values may vary and there may be some difference in the candidate’s answers and model answer.
6) In case of some questions credit may be given by judgement on part of examiner of relevant
answer based on candidate’s understanding.
7) For programming language papers, credit may be given to any other program based on
equivalent concept.

(Autonomous)
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Q.1 Any five
a) Define : 1 mark each
• i) Biochemistry: Biochemistry is the study of the chemical processes in living organisms.

It deals with the structure and function of cellular components such as proteins,
carbohydrates, lipids, nucleic acids and other biomolecules.
• ii) Metabolism: All biochemical changes that occur in biological system are grouped
together as metabolism./ Metabolism is the set of chemical reactions(Anabolic &
Catabolic) that occur in living organisms to maintain life
• iii) Anabolism: It’s a biosynthetic phase, uses energy to construct components of cells
such as proteins and nucleic acids.
• iv) Catabolism : It’s a process of degradation of complex matter into simple form thus
generating energy & metabolites that provide metabolic fuel & building block for the
cell.
b) Physiological functions: 2marks each (any 4 functions)
Minerals:
• Maintenance of acid base balance
• Maintenance of electrolyte balance
• Maintenance of osmotic pressure of cell
• Growth & maintenance of tissues & bones
• Proper working of nervous system
• Muscle contractions
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Subject Code: 0808 Model Answer Page No:3/ 40
• Transport of oxygen
• Activation of enzymes
Lipids:
• Energy storage : Triacylglycerols, stored in adipose tissue, are a major form of energy
storage in animals.
• Acting as structural components of cell membranes: The glycerophospholipids are the

main structural component of biological membranes,
• Dietary fats help to dissolve fat soluble vitamins:
• Humans have a requirement for certain essential fatty acids, such as linoleic acid.
• Lipids provide excellent insulation as fat is bad conductor of heat.
• Fats provide padding to protect internal organs.
c)Definition 1 mark, Classification of proteins 2 marks Egs 1 mark
Proteins are high molecular weight biomolecules, natural polymers composed of

long chains of subunits called amino acids joined through peptide linkage.
• Classification: Based on chemical nature
1.Simple proteins: Contain only amino acid residues
Protamines
Histones
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Subject Code: 0808 Model Answer Page No:4/ 40
Albumins & globulins
Scleropropteins
Albumins & globulins
Scleroproteins
2. Conjugated Proteins: Contain other substances or groups in addition to polypeptide

chains.
Nucleoproteins
Phosphoproteins
Glycoproteins
Lipoproteins
3. Derived Proteins: Contain products obtained on hydrolysis of simple & conjugated

proteins.
Proteins can also be classified on nutritional basis:
Complete proteins: Contain all essential amino acids in required quantities eg. Milk
protein, egg protein
Incomplete proteins: Don’t contain all essential amino acids. Eg. Gelatin, zein of maize
(Autonomous)
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d) Deficiency diseases; 1 mark each
i) Thiamine: Beri beri
ii) Niacin: Pellagra
iii) VitaminC: Scurvy
iv) Vitamin K: Blood clotting disorders, Haemorrhage
e) Benedict’s Test: Test 1 marks, reaction 1 mark, Principle 2 marks
Test: When sugar solution is heated with benedict’s reagent it gives red precipitate
Principle: Carbohydrate is heated with alkaline copper sulphate, copper ions get reduced
and give red precipitate of cuprous oxide. All reducing sugars give this test positive,
while sugars like sucrose does not give this test positive.
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f) Lipids: Defn..1 mark, Classificatin 3 marks
The lipids are a large and diverse group of naturally occuring organic compounds
that are related by their solubility in nonpolar organic solvents (e.g. ether,
chloroform, acetone & benzene) and general insolubility in water. They are esters of
fatty acids.
Classification:
• Simple
• Complex/ Compound
• Derived
• Miscellaneous
Neutral
Simple lipids:
Esters of fatty acids with alcohol.
• Fats & oils : Castor oil
• Waxes : Bees wax
Compound Lipid
• Glycerophospholipids., Sphingophospholipids, Glycolipids:.
• Lipoprotiens: Contain protiens
• Sulpholipids
• Aminolipids
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• Lipoprotiens: Contain protiens
• Sulpholipids:
• Aminolipids:
Derived Lipids:
• Eg: Alcohols, Glycerol, Fatty acids etc
Miscellaneous Lipids:
• Eg : Carotenoids, Squalene.
Neutral Lipids:
• They are mono, di, triacyl glycerols, cholesterol, cholesteryl esters.
g) Active site of enzyme; Defn 1 mark, Each model 1 mark, Diagram 1 mark
• Portion of an enzyme to which the substrate binds & gets converted into the product.
• In the active site ,the amino acids are grouped together in such a manner so as to enable
the enzymes to combine with substrate.
• Binding of substrate explained by 2 models:
Lock & key model
Induce fit model

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Lock & Key model:
It is the first model proposed by” Emil Fisher” to explain enzyme action mechanism.
It is like a Lock & Key.
In this case the shape of active site of an enzyme and that of substrate is complementary to each
other. The substrate molecule fits into the active site of enzyme just as key fits into a lock. Hence
called Lock & Key model.
The shape of active site is rigid and complementary to the shape of substrate complex.
Induced fit model:
In this case the shape of active site of an enzyme is flexible so as to accommodate wide variety
of substrate molecules.
The shape of active site of enzyme is made complementary to the substrate molecule.
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Q.2 : Any three
a) Definition 1 mark, Classification 2 mark, Examples 1 mark
Carbohydrates can be defined as polyhydroxy aldehyde or ketones or compounds derived from

them. General formula is Cn (H2O)n
Carbohydrates
Sugar Non-sugar
(saccharide) (polysaccharide)
Monosaccharide Disaccharide Oligosaccharide Homopolysaccharide Heteropolysaccharide
Triose - Maltose Raffinose Starch Agar
Tetrose Lactose Gentianose glycogen Alginate
Pentose Sucrose Cellulose Hyaluronic acid
Monosaccharides can be classified into following subtypes:
Aldose Ketose
Trioses Glyceraldehyde Dihydroxy acetone
Tetroses Erythrose Erythrulose
Pentoses Ribose Ribulose
Hexose Glucose Fructose

(Autonomous)
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b) Enumerate(any4) 2 marks, Ninhydrin reaction 2 mark
1. Biuret test
2. Xanthoproteic test
3. Millons test
4. Sakaguchi reaction
5. Nitroprusside test
i) Ninhydrin reaction:
In acidic condition amino acid reacts with ninhydrin to give blue to violet colour, at 60-70 0C.
(Reaction is optional )
Ninhydrin Amino acid
A deep blue or purple color known as Ruhemann's purple is evolved. It’s an identification test
for amino acids
Ninhydrin is most commonly used to detect fingerprints.

(Autonomous)
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c) Diseases related to lipid metabolism (any 4)
1. Obesity is due to accumulation of excess of body fat
2. Lipidosis abnormal lipoproteins in blood or specific lipids in blood tissue
3. Hyperlipidemia: Increase in plama cholesterol or plasma triglycerides
4. Hyperlipoprotenemia: increase in lipoproteins.
5. Ketosis: Formation of ketone bodies
6. Lipid storage diseases (Enlargement of liver and spleen, leads to mental retardation)
• Niemann pick disease
• Gaucher’s disease
• Metachromatic leukdystrophy
d) Essential and non essential amino acids (Definition 1mark Example 1 mark each)
Essential amino acids: Amino acids which cannot be synthesized by the body but which are
required for normal functioning of body and supplied through diet.
Eg. Valine, leuciene, Isoleucine, phenylalanine, tryptophan, lysine, arginine, histidine,

methonine. (any 2)
Non essential amino acids: Amino acids which are synthesized in the body
Eg. Glycine, alanine, tyrosine, aspargine, aspartic acid , glutamine, glutamic acid, cysteine,
serine, proline (any 2)
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e) Anaemia: Defn 1 mark, Types (any 4) 1 mark, Expln of megaloblastic anaemia 2 marks
Decrease in oxygen carrying capacity of blood can be called as anaemia. It depends

on haemoglobin content of erythrocytes .Reduction in blood haemoglobin level &
number of circulating erythrocytes indicates anaemia.
Types of anaemia
1. Pernicious anaemia
2. Sickle cell anaemia
3. Iron deficiency anaemia
4. Aplastic anaemia
5. Haemolytic anaemia
Megaloblastic anaemia-
It is also called as pernicious anaemia or macrocytic anaemia. In this type of anaemia essential
factors are absent which are required for the formation of RBC. So RBC count is decreased i.e.
intrinsic factors responsible for absorption of vitamin B12 from gastric acid is absent.
This type of anaemia occurs due to deficiency of either vit.B12 or folic acid .In the deficiency of
either of them, the maturation of red blood cell does not occur. As a result no. of erythrocytes
goes down and their average size is increased. Immature large sized red blood cells are called
megaloblast and are released in circulation
Symptoms: nervousness, numbness, tingling, occurrence of pins & needles.

(Autonomous)
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Q.3 Solve any three 3*4 =12
a) Define enzyme & classify them with examples: Defn 1 mark, Classification 3 marks
Highly specific proteinous substances that are synthesized in a living cell & catalyze or speed up
the thermodynamically possible reactions necessary for their existence.
Classification Of Enzymes:
On the basis of site of action:
Exoenzymes / Extracellular enzymes:
• Secreted outside the cell
• Decompose complex organic matter like proteins ,fats, cellulose .E.g..: proteoses, lipases.
Endoenzymes / Intracellular enzymes:
• Present inside the cell
• E.g..: synthetases, phosphorylases
Constitutive Enzymes:
• Produced in absence of substrate.Eg.: Enzymes of glycolytic series.
Induced Enzymes:
• Produced in presence of substrate.Eg.: hepatic microsomal enzymes.
Zymogens / Proenzymes:
• Produced naturally in an inactive form whch can be activated when required. Enzymes
like pepsin are created in the form of pepsinogen, an inactive zymogen. Pepsinogen is
activated when Chief cells release it into HCl which partially activates it.
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OR
Classification of Enzymes on the basis of reactions they catalyze:
• Oxidoreductases :
They bring about biological oxidation & reduction between two substrates.
e.g ; Dehydrogenases, Oxidases, Hydroperoxidases, Oxygenases, Hydroxylases
• Transferases :
Catalyse transfer of some group or radical from one molecule to another.
E.g.Transaminases, Transphosphorylases, Transglycosidases
• Hydrolases:
Bring about hydrolysis or condensation of substrate by addition or removal of water.
Eg. Esterases, Peptidases
Lysases:
• Catalyse removal of groups from larger substrates by mechanisms other than hydrolysis,
leaving double bonds.
e.g. Carboxylysases, Aldehydelysases
Isomerases:
Catalyze interconversion of isomers. eg. Dextrose isomerase
Ligases/ Synthatases:
• Catalyse the linking or synthesizing together of 2 compounds. Forming C-S bonds, C-N
bonds, C-C bonds. E.g: Lysases, Isomerases, Ligases / Synthatases
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b ) Protein metabolism diseases (Enlist 1 mark, Explanation(any3) 3 marks)
1. Phenylketouria: This is a genetic disorder related to phenyalanine metabolism.

Phenyalanine is precursor for biosynthsis of tyrosine. In the catabolism of phenyl alanine
the first enzyme phenylalanine hydroxylase convert phenylalanine to tyrosine. The
inherited deficiency of this enzyme results in accumulation of phenyl alanine, and is
excreted as phenyl pyruvate. This condition is called phenyl ketouria.
2. Alkaptonuria: This is a metabolic disorder of phenyl alanine due to lack of enzyme

homogentisate deoxygenase resulting into accumulation of homogentisate, which is
excreted via urine.
3. Maple syrup urine disease: It is also called as branched chain ketoaciduria. The disease
which is caused due to absence or highly reduced activity of branched chain alpha-
ketohydrogenase complex is called as maple syrup urine disease. As a result amino acids
accumulate in the blood and excreted in urine.
4. Hartnup’s disease:
It is a metabolic disorder of tryptophan catabolism. Deficiency of tryptophan pyrrolase

results into accumulation of tryptophan and its derivatives indolacetic acid, indolepyruvic
acid etc.
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c) Write sources, biological active form and role of vit A in vision.(0.5 marks for source and
active form and Diagram 1 mark, explanation 2 marks)
Sources: Carotenoids, fish liver oil, milk, egg, fruits, Corn and apricot.
Biological active form: Vitamin A1 ( Retinol) and Vitamin A2 (Dehydroretinol)
Role
The retina of the eye contains two types of receptor cells, Rod cells which are responsible for
dim light vision & the cones, responsible for bright light vision .Cones are also responsible for
colour perception. The deficiency of cone pigments makes the individual colour blind.
In retinal pigments, the rod cells contain rhodopsin. Under the influence of light, rhodopsin is
converted to lumirhodopsin which is further converted into metarhodopsin.
Then hydrolysed to protein opsin & trans retinal. Trans-Retinal(trans- retinene) is inactive in the
synthesis of rhodopsin, it must be coverted to the active cis- isomer.
In the eye, the trans-retinal is reduced to trans-retinol by the enzyme retinal reductase & NADH.
The trans retinol which is too inactive in rhodopsin synthesis is passed into blood stream, then
carried to liver .
It is then converted to cis -isomer. In dim light active cis-retinol from the blood enters the retina
where it is oxidized to cis-retinal by reverse action of retinal reductase in the presence of NAD+.
Finally the cis-retinal combines with protein opsin to give back rhodopsin and thus cycle is
repeated.
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Rhodopsin
Lumi- rhodopsin
Dark
Meta- rhodopsin
Opsin cis-retinal Blue light Trans- retinal + opsin

(active) Retinol isomerase (inactive )
NADH+H+
NADH +H+
Cis-retinol
(active) Trans -retinal
(inactive)
Blood retinol LIVER

RETINOL
The individual having vitamin A deficiency are unable to resynthesise rhodopsin and thus unable
to see in the dim light and the condition is called night blindness.
(Autonomous)
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d) Define: (1 mark for each definition).
i) Rancidity: Fats and oils are exposed to light, air, heat, moisture for a longer time, develops
disagreeable and objectionable odour. Such oil or fat is said to be rancid, and the phenomenon is
called as rancidity
ii) Sap value: It is the number of milligrams of KOH required to saponify free or combined
fatty acids present in 1 gram of fat or oil.
iii) Reichert-meissel number: It is the number of mililitres of alkali required to neutralize the
soluble volatile fatty acids from 5g of fat or oil.
iv) Acid value: It is the number of milligram of KOH required to neutralize the free fatty acids
present in 1 gram of fat or oil.
e) Define Physiological and Pathological urine? (Definition 1 mark each, 2 marks abnormal
constituents any four)
Physiological urine
Urine that contains the waste products like uric acid, urea, creatinine and certain salts such as
chlorides and sulphates substances which are not required by the body or tissues.
Pathological urine
Urine that contains substances essential to the body or tissues (like sugar, bile salts, albumin
etc.), in addition to normal organic & inorganic substances, is called as pathological or abnormal
urine. Such urine indicates some disease or disorder or derailment in body physiology.
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Abnormal constituents
Associated ailment
Sugar (glucose) Glycosuria- Diabetes mellitus
Ketone bodies Ketonuria- Diabetis mellitus, Preganancy,

Carbohydrate starvation
Albumin Proteinuria- Pregnancy, severe exercise, high

protein meal, Nephritis
Bile pigments / salts Jaundice /Hepatitis
Blood Haematuria- Acute inflammation of urinary

organs, T.B., Cancer, Haemolytic jaundice etc.
Pus Pyuria- Inflammation of urinary bladder,

urethra, kidney
Q.4.
a) Define Vitamins. Write its classification (definition 1 mark, Classification 2marks,

example 1 mark)
The naturally occurring micronutrients present in food and are required for normal functioning
and growth of the living organisms are called as a vitamins.
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Classification
• Fat soluble vitamins: these are soluble in fat and are stored in liver. Their absorption
requires presence of bile salts and fats.
a) Vitamin A
b) Vitamin D
c) Vitamin E
d) Vitamin K
• Water soluble vitamins: These are soluble in water and are not stored in body. Water
soluble vitamin includes B-complex group and vitamin C.
B complex
a) Vitamin B1- Thiamine
b) Vitamin B2- Riboflavin
c) Vitamin B3- Niacine
d) Vitamin B5- Pantothenic acid
e) Vitamin B6- Pyridoxine
f) Vitamin B7- Biotin
g) Vitamin B9- Folic acid
h) Vitamin B12- Cyanocobalamin
Non B- complex: Vitamin C (Ascorbic acid)

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b) Enumerate various factors affecting the enzymatic reaction. Explain the effect of
temperature and pH with the help of curves. ( Enumerate 1 mark, Expln of factor 1.5 each)
• Hydrogen ion concentration
• Concentration of enzymes
• Concentration of substrate
• Temperature
• Time
• Products of reaction
• Effect of light & other physical factors
• Allosteric factors
• Effect of hormones & other biochemical agents
Effect of temperature :( 1.5 mark)
• Optimum temperature is usually reached at around 37oC—45oC for animal enzymes.
• Velocity of reaction is increased from 1.1 to 3 times for every 10o rise in temperature.
• Above the optimum temperature, rate decreases.
• The enzyme gets denatured at a rate faster than the increase in reaction.
• Most of the enzymes get denatured above 60oC.
• The time of exposure is also important factor. An enzyme may withstand higher
temperatures for short periods of time.
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• Optimum temperature has meaning only if the time of reaction is also stipulated. Enzyme
activity is maximum at optimum temperature.
Effect of pH: 1mark( any other valid graph)
• Enzyme reactions are influenced by varying H ion concentration.
• The optimum pH is that pH at which a certain enzyme causes a reaction to progress most
rapidly.
• On either side of the optimum, the rate of reaction is lower & at certain pH enzyme may
be inactivated or even destroyed.
• Buffers are used to keep enzyme at an optimum or at least a favorable H ion

concentration.
• Optimum pH is dependent on kind of buffer, particular substrate, source of enzyme.
Eg.: optimum pH of sucrase is 6.2, pepsin is 1.5- 2.5

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c) Write a biochemical role and deficiency diseases (0.5 for any one function and 0.5 for any
one disease)
I. Iron
Functions
• It is required for the formation of red blood cells.
• It is involved in oxygen transportation
• It acts as a electron carrier
• It is involved in DNA synthesis.
Diseases
• Anaemia
II. Calcium
Functions
• It is required for formation and development of bones and teeth
• It is required for blood coagulation process
• It is required for regulation of muscle contraction
Diseases
• Rickets
• Osteoporosis
• Tetany
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III. Iodine
Fuctions
• Iodine is essential trace element required for the biosynthesis of thyroid hormones like
thyroxine and triiodothyronine.
• It is required for the normal growth and development of body.
• About one third of the total body iodine is in thyroid gland, remaining is distributed in
ovary, muscles, blood and all tissues.
Diseases
• Goitre / Hypothyroidism
IV. Cobalt
Functions
• It acts as a co-factor for several enzymes
• It is present in vitamin B12
• It helps in erythropoiesis
Diseases
• Anaemia
(Autonomous)
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d) Write the classification of amino acids with example
Amino acids are obtained from protein by hydrolysis, catalysed by acid, base or enzymes
such as pepsin, trypsin.
OR
Amino acids- these are a group of organic compounds containing two functional groups,
amino group and carboxyl group.
Classification of amino acids:

1) Neutral amino acid.
2) Acidic amino acid.
3) Basic amino acid.
1) Neutral:
(a) Aliphatic amino acids:
e .g. Glycine, Alanine
(b) Aromatic amino acids:
e. g. Phenyl alanine, tyrosine
(c) Heterocyclic amino acids/Imino acids
e. g. Proline, Hydroxy proline
(d) Sulphur containing amino acids:
e.g. Cysteine, Methionine.
(e) Amino acid containing hydroxyl group:
e.g. Serine, Threonine
2) Acidic amino acids:
e.g. Aspartic acid, Aspargine.
3) Basic amino acids:
e.g. Arginine, Lysine
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e) Write in detail about Osazone test

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Explanation:
i. When reducing sugar (glucose) is treated with phenyl hydrazine, it gives reaction product
(glucose) phenylhydrazone.
ii. Two molecules of phenyl hydrazine are heated again with (glucose) phenylhydrazone, it
gives products like ammonia, aniline, (glucosazone) osazone.
Significance:
i. Osazone test helps to differentiate reducing sugars from non reducing sugars like starch,
dextrin, sucrose.
ii. It also helps in differentiating particular type of reducing sugars.
iii. It is used to identify and confirm reducing sugars, e.g. glucose, fructose, galactose,
maltose, lactose.

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Question 5: Solve any 3
a) Explain water balance of body ( explanation 2 marks, sheet 2marks)

(Balance may be given for 2500ml/2800ml)
Water is very essential for living system. There is no life without water. Total body water
accounts for 70%of body weight. However a loss of 10% of water in our body is serious
and a loss of 20% is fatal.
Therefore a balance should be maintained between water intake and output.
Water intake source -
1) Drinking water -1500ml
2) Solid food -1000ml
3) Oxidation of carbohydrates , fats and protein- 300ml
Water loss from body -
Water is lost continuously from the body in the following ways.
1) via kidney as urine -1500ml
2) via skin -800ml
3) via lungs in expired air -400ml
4) via feces- 100ml
Water intake Ml Water loss Ml
Drinking water 1500ml Urine 1500ml
Solid food 1000ml Feces 100ml
Oxidation of carbohydrates, 300ml Skin 800ml
Fats, Proteins lungs 400ml
Total 2800ml 2800ml

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b) Define following terms( each 1 mark)

i. Pathology
It is branch of science that deals with study of diseases OR
The science of the causes and effects of diseases, especially the branch of
medicine that deals with the laboratory examination of samples of body
tissue for diagnostic or forensic purposes
ii. Cofactor
Co- factor- the non-protein moiety / metal for catalytic activity is
generally called as co-factor
iii. Abnormal metabolism
Almost all biochemical reactions of cell or organism are catalyzed by
number of enzymes and other factors, the deficiency of these enzymes or
some other factors like vitamins and minerals may lead to abnormal
metabolic reactions this is called abnormal metabolism.
iv. Coenzymes
These are organic molecules, often derived from the B-complex group
vitamins that participate directly in enzymatic reactions.
OR
Co-enzymes may be defined as substance necessary for the activity of
certain enzymes.

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c)Write various diseases related to carbohydrates metabolism ( Enlist 1 mark,
explanation of any 3 for 3 marks)
i)Diabetes mellitus ii) glycogen storage diseases iii) glycosuria
i)Diabetes mellitus –it is a metabolic disorder in which body is unable to utilize the
glucose.
It is characterized by hyperglycaemia, glycosuria, polyuria, polydipsia ,polyphagia

,ketosis, loss of weight, light color of urine
Types of DM
Insulin dependent diabetes mellitus
Non Insulin dependent diabetes mellitus
ii) Glycogen storage diseases-
these diseases are referred to as the diseases caused by accumulation of polysaccharide I

.e. glucose progressive cirrhosis of lever cells produce a condition in which glycogen
does not get converted to glucose and hence glycogen in blood goes on increasing.
It is group of disorder like I)Van G ierke,s disease ii) Pomp,es diseases iii)Limit
dextinosis iv) Amylopectinosis. (Optional)
iii)Glycosuria- Apperance of usually high amount of glucose in the urine is called as

glycosuria
iv) Galactosemia- Due to deficiency of enzyme galactose 1 phosphate uridyl transferase

and galactokinase which increases galactose concentration leading to cataract.
v) fructose intolerance: High concentration of fructose in blood.
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d)Explain role of lipids in biological membrane (explanation 2 marks ,diagram

2marks)
The major component of biological membrane is phospholipid. Phospholipid has 2 long
chains of hydrocarbon of fatty acids. The chains are hydrophobic and have strong polar
group i.e. phosphate at 3rd carbon of glycerol. When phospholipids are added to aqueous
medium they form micelles, monolayer & bilayer, depending on the concentration of
phospholipids. The hydrophilic & hydrophobic interaction of phospholipids is forming
bilayer in water. Hydrophobic tails are hidden from aqueous environment and form an
internal hydrophobic phase where as hydrophilic heads are exposed to the surface.
Bilayer system of this type is extensively studied as model of natural membrane.

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Biomembranes are made up phospholipids lipoproteins, glycoproteins and proteins all these
components are assembled together by non covalent interactions

e)Give structure and two tests of cholesterol.( stru. 1 marks, any 2 tests 3marks)

1)Liebermann-Burchard test:
When chloroform solution of cholesterol is treated with acetic anhydride &

concentrated sulphuric acid, green colour is formed.
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2)Salkowaski test:
When chloroform solution of cholesterol is treated with concentrated sulphuric

acid, upper layer gives red colour and H2$O4 layer gives green colour.
3) Formaldehyde-H2SO4 Test:
To a solution of cholesterol in chloroform in dry test tube if formaldehyde-

sulphuric acid solution is added, cherry colour develops.

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Glycolysis: ( Detailed diagramatic representation can be considered for full marks)
It’s a main pathway for glucose oxidation
1. Phosphorylation of glucose to glucose 6 phospate in presece ofenzyme
hexokinase & ATP & Mg
2. Isomerisation of Glucose 6 phosphate to fructose 6 phosphate in presence of
phosphohexo isomerase
3. Phosphorylation of fructose 6 phosphate to fructose 1,6 diphosphate in presence
of phosphofructokinase,ATP & Mg
4. Cleavage of fructose 1,6 diphosphate to dihydroxy acetone phosphate &
glyceraldehyde 3 phosphate in presence of aldolase. These 2 products are
interconvertible in presence of triose phosphate isomerase
5. Glyceraldehyde 3 phosphate further undergoes oxidation to 1,3
diphosphoglycerate in presence of
glyceraldehyde 3 phosphate dehydrogenase & NAD+
6. Transformation of 1,3 diphosphoglycerate to 3- phosphoglycerate in presence of
phosphoglycerate kinase, Mg & ADP
7. 3- phosphoglycerate changes to 2-phosphoglycerate in presence of
phosphoglycerate mutase
8. Loss of water molecule from 2-phosphoglycerate results into formation of
phosphoenol pyruvic acid in presence of enolase
9. Loss of phosphate from phosphoenol pyruvic acid results into formation of Enol
pyruvic acid in presence of pyruvate kinase, Mg & ADP
10. Enol pyruvic acid gets converted to keto form of pyruvic acid in presence of
pyruvate kinase
11. Keto pyruvic acid under aerobic conditions enter TCA cycle in mitochondria.
Pyruvic acid forms main end product of glycolysis in those tissues which are
supplied with sufficient Oxygen
12. But tissues where oxygen is not supplied ,lactic acid is formed as an end product
of glycolysis by reduction in presence of lactate dehydrogenase & NADH
Net reaction for glycolysis is:
Glucose + 2NAD+ + 2 ADP + 2 Pi → 2 Pyruvate + 2 ATP + 2 NADH + 2 H2O
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b Explain kreb s Cycle ( Detailed diagramatic representation can be considered for full marks)

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Kreb’s cycle:
It’s a central pathway for release of energy from acetyl CoA whch is produced from
glycolysis, catabolism of fatty acids or amino acids
Steps:
1. Condensation of acetylCoA obtained from pyruvic acid with oxaloacetate to form
citric acid in presence of citrate synthatase
2. Conversion of citric acid to cis aconitate in presence of aconitase &fe2+
3. Cis aconitate accepts water to give isocitric acid in presence of aconitase & Fe2+
4. Isocitric acid undergoes oxidation in presence of isocitric dehydrogenase &
NAD+ to give Oxalosuccinic acid
5. Decarboxylation of oxalosucccinic acid to alpha ketoglutaric acid in presence of
isocitri dehydrogenase, Mg/ Mn
6. Oxidative decarboxylation of alpha ketoglutaric acid to succinyl CoA in presence
of alpha keto glutarate dehydrogenase, CoA-SH, NAD+, Mg
7. Succinyl Coa gets converted to succinic acid in presence of succinate thiokinase,
GDP, Mg
8. Succinic acid undergoes dehydrogenation in presence of succcinate
dehydrogenase, FAD+ to form fumaric acid
9. Fumaric acid takes up water molecule in presence of fumarase to form maleic
acid
10. Maleic acid undergoes oxidation in presence of malate dehydrogenase, NAD+ to
form oxaloacetic acid.
11. Cycle gets repeated again by entrance of another molecule of Acetyl CoA
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c)Explain Urea Cycle ( Detailed diagramatic representation can be considered for

full marks)

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Subject Code: 0808 Model Answer Page No: 39/40
1) Molecule of ammonia, CO2 & phosphate are condensed to form

‘Carbamoyl phosphate’ in presence of enzyme ‘carbamoyl-phosphate
synthetase.
2) Carbamoyl phosphate transferred to ornithine forms citrulline in
presence of an enzyme ornithine transcarbamoylase. This reaction takes
place in mitochondria. The citruline formed in this reaction enters in
cytoplasm & the next reactions take place in cytoplasm
3) Citrulline condenses with Aspartate to form argininosuccinate. The
reaction is catalysed by an enzyme Arginosuccinate synthetase.
4) Argininosuccinate is now cleaved into ‘arginine’ & ‘fumarate’ by the
enzyme ‘arginosuccinase’. Fumarate formed may be converted to
oxaloacetate via the actions of enzymes ‘fumerase’& malate
dehydrogenase & then transmitted to regenerate aspartate.
5) Finally arginine is cleaved into ornithine & urea by the enzyme arginase.
With this reaction cycle is completed & ornithine molecule accepts
molecule of carbamoyl phosphate to repeat the cycle.
The overall equation of the urea cycle is:
NH3 + CO2 + aspartate + 3 ATP + 2 H2O → urea + fumarate + 2 ADP
+ 2 Pi + AMP + PPi

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808

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MAHARASHTRA STATE BOARD OF TECHNICAL EDUCATION

Important Instructions to examiners:

Q.1 Any five

a) Define : 1 mark each

• i) Biochemistry: Biochemistry is the study of the chemical processes in living organisms.

b) Physiological functions: 2marks each (any 4 functions)

• Maintenance of electrolyte balance

• Maintenance of osmotic pressure of cell

• Growth & maintenance of tissues & bones

• Proper working of nervous system

• Acting as structural components of cell membranes: The glycerophospholipids are the

• Dietary fats help to dissolve fat soluble vitamins:

• Lipids provide excellent insulation as fat is bad conductor of heat.

• Fats provide padding to protect internal organs.

c)Definition 1 mark, Classification of proteins 2 marks Egs 1 mark

Proteins are high molecular weight biomolecules, natural polymers composed of

• Classification: Based on chemical nature

1.Simple proteins: Contain only amino acid residues

Albumins & globulins

Albumins & globulins

2. Conjugated Proteins: Contain other substances or groups in addition to polypeptide

3. Derived Proteins: Contain products obtained on hydrolysis of simple & conjugated

Proteins can also be classified on nutritional basis:

d) Deficiency diseases; 1 mark each

i) Thiamine: Beri beri

ii) Niacin: Pellagra

iii) VitaminC: Scurvy

iv) Vitamin K: Blood clotting disorders, Haemorrhage

e) Benedict’s Test: Test 1 marks, reaction 1 mark, Principle 2 marks

f) Lipids: Defn..1 mark, Classificatin 3 marks

Esters of fatty acids with alcohol.

• Fats & oils : Castor oil

• Waxes : Bees wax

• Glycerophospholipids., Sphingophospholipids, Glycolipids:.

• Lipoprotiens: Contain protiens

• Lipoprotiens: Contain protiens

• Eg: Alcohols, Glycerol, Fatty acids etc

• They are mono, di, triacyl glycerols, cholesterol, cholesteryl esters.

• Binding of substrate explained by 2 models:

Lock & key model

Lock & Key model:

It is like a Lock & Key.

Induced fit model:

Q.2 : Any three

a) Definition 1 mark, Classification 2 mark, Examples 1 mark

Carbohydrates can be defined as polyhydroxy aldehyde or ketones or compounds derived from

Monosaccharide Disaccharide Oligosaccharide Homopolysaccharide Heteropolysaccharide

Triose - Maltose Raffinose Starch Agar

Tetrose Lactose Gentianose glycogen Alginate

Pentose Sucrose Cellulose Hyaluronic acid

Monosaccharides can be classified into following subtypes:

Trioses Glyceraldehyde Dihydroxy acetone

Tetroses Erythrose Erythrulose

Pentoses Ribose Ribulose

Hexose Glucose Fructose

b) Enumerate(any4) 2 marks, Ninhydrin reaction 2 mark

Ninhydrin Amino acid

Ninhydrin is most commonly used to detect fingerprints.

c) Diseases related to lipid metabolism (any 4)

1. Obesity is due to accumulation of excess of body fat

2. Lipidosis abnormal lipoproteins in blood or specific lipids in blood tissue

3. Hyperlipidemia: Increase in plama cholesterol or plasma triglycerides

4. Hyperlipoprotenemia: increase in lipoproteins.