Hello friends, in today's article we see mcq's of proteins in biotechnology field. so let's begin
Proteins MCQ’s
1. All
proteins contain the
(A) Same 20 amino acids
(B) Different amino acids
(C) 300 Amino acids occurring in nature
(D) Only a few amino acids
2.
Proteins contain
(A) Only L- α - amino acids
(B) Only
D-amino acids
(C) DL-Amino
acids
(D) Both (A)
and (B)
3. The
optically inactive amino acid is
(A) Glycine
(B) Serine
(C) Threonine
(D) Valine
4. At
neutral pH, a mixture of amino acids in solution would be predominantly:
(A) Dipolar ions
(B) Nonpolar
molecules
(C) Positive
and monovalent
(D) Hydrophobic
5. The
true statement about solutions of amino acids at physiological pH is
(A) All amino acids contain both positive and
negative charges
(B) All amino acids
contain positively charged side chains
(C) Some amino
acids contain only positive charge
(D) All amino
acids contain negatively charged side chains
6. pH
(isoelectric pH) of alanine is
(A) 6.02
(B) 6.6
(C) 6.8
(D) 7.2
7. Since
the pK values for aspartic acid are 2.0, 3.9 and 10.0, it follows that the isoelectric
(pH) is
(A) 3.0
(B) 3.9
(C) 5.9
(D) 6.0
8.
Sulphur containing amino acid is
(A) Methionine
(B) Leucine
(C) Valine
(D) Asparagine
9. An
example of sulphur containing amino acid is
(A)
2-Amino-3-mercaptopropanoic acid
(B) 2-Amino-3-methylbutanoic acid
(C) 2-Amino-3-hydroxypropanoic acid
(D) Amino acetic acid
10. All
the following are sulphur containing amino acids found in proteins except
(A) Cysteine
(B) Cystine
(C) Methionine
(D) Threonine
11. An
aromatic amino acid is
(A) Lysine
(B) Tyrosine
(C) Taurine
(D) Arginine
12. The
functions of plasma albumin are
(A) Osmosis
(B) Transport
(C) Immunity
(D) both (A
)and (B)
13. Amino
acid with side chain containing basic groups is
(A) 2-Amino 5-guanidovaleric acid
(B) 2-Pyrrolidine
carboxylic acid
(C) 2-Amino
3-mercaptopropanoic acid
(D) 2-Amino
propanoic acid
14. An
example of α-amino acid not present in proteins but essential in mammalian metabolism
is
(A) 3-Amino
3-hydroxypropanoic acid
(B) 2-Amino
3-hydroxybutanoic acid
(C) 2-Amino 4-mercaptobutanoic acid
(D) 2-Amino
3-mercaptopropanoic acid
15. An
essential amino acid in man is
(A) Aspartate
(B) Tyrosine
(C) Methionine
(D) Serine
16. Non
essential amino acids
(A) Are not
components of tissue proteins
(B) May be synthesized in the body from essential
amino acids
(C) Have no
role in the metabolism
(D) May be
synthesized in the body in diseased states
17. Which
one of the following is semi essential amino acid for humans?
(A) Valine
(B) Arginine
(C) Lysine
(D) Tyrosine
18. An
example of polar amino acid is
(A) Alanine
(B) Leucine
(C) Arginine
(D) Valine
19. The
amino acid with a nonpolar side chain is
(A) Serine
(B) Valine
(C) Asparagine
(D) Threonine
20. A
ketogenic amino acid is
(A) Valine
(B) Cysteine
(C) Leucine
(D) Threonine
21. An
amino acid that does not form an α-helix is
(A) Valine
(B) Proline
(C) Tyrosine
(D) Tryptophan
22. An
amino acid not found in proteins is
(A) β-Alanine
(B) Proline
(C) Lysine
(D) Histidine
23. In
mammalian tissues serine can be a biosynthetic precursor of
(A) Methionine
(B) Glycine
(C) Tryptophan
(D)
Phenylalanine
24. A
vasodilating compound is produced by the decarboxylation of the amino acid:
(A) Arginine
(B) Aspartic
acid
(C) Glutamine
(D) Histidine
25.
Biuret reaction is specific for
(A)
-CONH-linkages
(B) -CSNH2 group
(C) -(NH)NH2
group
(D) All of
these
26.
Sakaguchi’s reaction is specific for
(A) Tyrosine
(B) Proline
(C) Arginine
(D) Cysteine
27.
Million-Nasse’s reaction is specific for the amino acid:
(A) Tryptophan
(B) Tyrosine
(C)
Phenylalanine
(D) Arginine
28.
Ninhydrin with evolution of CO2 forms a blue complex with
(A) Peptide
bond
(B) α -Amino acids
(C) Serotonin
(D) Histamine
29. The
most of the ultraviolet absorption of proteins above 240 nm is due to their content
of
(A) Tryptophan
(B) Aspartate
(C) Glutamate
(D) Alanine
30. Which
of the following is a dipeptide?
(A) Anserine
(B) Glutathione
(C) Glucagon
(D) β
-Lipoprotein
31. Which
of the following is a tripeptide?
(A) Anserine
(B) Oxytocin
(C) Glutathione
(D) Kallidin
32. A
peptide which acts as potent smooth muscle hypotensive agent is
(A) Glutathione
(B) Bradykinin
(C) Tryocidine
(D)
Gramicidin-s
33. A
tripeptide functioning as an important reducing agent in the tissues is
(A) Bradykinin
(B) Kallidin
(C) Tyrocidin
(D) Glutathione
34. An
example of metalloprotein is
(A) Casein
(B) Ceruloplasmin
(C) Gelatin
(D) Salmine
35.
Carbonic anhydrase is an example of
(A) Lipoprotein
(B) Phosphoprotein
(C) Metalloprotein
(D)
Chromoprotein
36. An
example of chromoprotein is
(A) Hemoglobin
(B) Sturine
(C) Nuclein
(D) Gliadin
37. An
example of scleroprotein is
(A) Zein
(B) Keratin
(C) Glutenin
(D) Ovoglobulin
38.
Casein, the milk protein is
(A)
Nucleoprotein
(B)
Chromoprotein
(C) Phosphoprotein
(D)
Glycoprotein
39. An
example of phosphoprotein present in egg yolk is
(A) Ovoalbumin
(B) Ovoglobulin
(C) Ovovitellin
(D) Avidin
Read more carbohydrates MCQ's
40. A
simple protein found in the nucleoproteins of the sperm is
(A) Prolamine
(B) Protamine
(C) Glutelin
(D) Globulin
41.
Histones are
(A) Identical
to protamine
(B) Proteins rich in lysine and arginine
(C) Proteins
with high molecular weight
(D) Insoluble
in water and very dilute acids
42. The
protein present in hair is
(A) Keratin
(B) Elastin
(C) Myosin
(D)
Tropocollagen
43. The
amino acid from which synthesis of the protein of hair keratin takes place is
(A) Alanine
(B) Methionine
(C) Proline
(D) Hydroxyproline
44. In
one molecule of albumin the number of amino acids is
(A) 510
(B) 590
(C) 610
(D) 650
45.
Plasma proteins which contain more than 4% hexosamine are
(A)
Microglobulins
(B)
Glycoproteins
(C) Mucoproteins
(D)
Orosomucoids
46.
After releasing O2 at
the tissues, hemoglobin
transports
(A) CO2 and protons to the lungs
(B) O2
to the lungs
(C) CO2
and protons to the tissue
(D) Nutrients
47.
Ehlers-Danlos syndrome characterized by hypermobile joints and skin
abnormalities is due to
(A) Abnormality in gene for procollagen
(B) Deficiency
of lysyl oxidase
(C) Deficiency
of prolyl hydroxylase
(D) Deficiency
of lysyl hydroxylase
48.
Proteins are soluble in
(A) Anhydrous
acetone
(B) Aqueous alcohol
(C) Anhydrous
alcohol
(D) Benzene
49. A
cereal protein soluble in 70% alcohol but insoluble in water or salt solution
is
(A) Glutelin
(B) Protamine
(C) Albumin
(D) Gliadin
50. Many
globular proteins are stable insolution inspite they lack in
(A) Disulphide bonds
(B) Hydrogen
bonds
(C) Salt bonds
(D) Non polar
bonds
51. The
hydrogen bonds between peptide linkages of a protein molecules are interfered
by
(A) Guanidine
(B) Uric acid
(C) Oxalic acid
(D) Salicylic
acid
52.
Globular proteins have completely folded, coiled polypeptide chain and the
axial ratio (ratio of length to
breadth) is
(A) Less than 10 and generally not greater than
3-4
(B) Generally
10
(C) Greater
than 10 and generally 20
(D) Greater
than 10
53.
Fibrous proteins have axial ratio
(A) Less than
10
(B) Less than
10 and generally not greater than 3-4
(C) Generally
10
(D) Greater than 10
54. Each
turn of α -helix contains the amino acid residues (number):
(A) 3.6
(B) 3.0
(C) 4.2
(D) 4.5
55.
Distance traveled per turn of α−helix in nm is
(A) 0.53
(B) 0.54
(C) 0.44
(D) 0.48
56. Along
the α-helix each amino acid residue advances in nm by
(A) 0.15
(B) 0.10
(C) 0.12
(D) 0.20
57. The
number of helices present in a collagen molecule is
(A) 1
(B) 2
(C) 3
(D) 4
58. In
proteins the α-helix and β-pleated sheet are examples of
(A) Primary
structure
(B) Secondary structure
(C) Tertiary
structure
(D) Quaternary
structure
59. The
a-helix of proteins is
(A) A pleated
structure
(B) Made
periodic by disulphide bridges
(C) A non-periodic structure
(D) Stabilised
by hydrogen bonds between NH and CO groups of the main chain
60. At
the lowest energy level α-helix of polypeptide chain is stabilised
(A) By hydrogen bonds formed between the H of
peptide N and the carbonyl O of the residue
(B) Disulphide bonds
(C) Non polar
bonds
(D) Ester bonds
61. Both
α-helix and β-pleated sheet conformation of proteins were proposed by
(A) Watson and
Crick
(B) Pauling and Corey
(C) Waugh and
King
(D) Y.S.Rao
62. The
primary structure of fibroin, the principal protein of silk worm fibres consists
almost entirely of
(A) Glycine
(B) Aspartate
(C) Keratin
(D) Tryptophan
63.
Tertiary structure of a protein describes
(A) The order
of amino acids
(B) Location of disulphide bonds
(C) Loop
regions of proteins
(D) The ways of protein folding
64. In a
protein molecule the disulphide bondis not broken by
(A) Reduction
(B) Oxidation
(C) Denaturation
(D) X-ray
diffraction
65. The
technique for purification of proteins that can be made specific for a given protein
is
(A) Gel
filtration chromotography
(B) Ion
exchange chromatography
(C)
Electrophoresis
(D) Affinity chromatography
66.
Denaturation of proteins results in
(A) Disruption
of primary structure
(B) Breakdown
of peptide bonds
(C) Destruction of hydrogen bonds
(D)
Irreversible changes in the molecule
67.
Ceruloplasmin is
(A) α1-globulin
(B) α2-globulin
(C) β-globulin
(D) None of
these
68. The
lipoprotein with the fastest electrophoretic mobility and the lowest triglyceride
content is
(A) Chylomicron
(B) VLDL
(C) IDL
(D) HDL
69. The
lipoprotein associated with activation of LCAT is
(A) HDL
(B) LDL
(C) VLDL
(D) IDL
70. The
apolipoprotein which acts as activator of LCAT is
(A) A-I
(B) A-IV
(C) C-II
(D) D
71. The
apolipoprotein which acts as actiator of extrahepatic lipoprotein is
(A) Apo-A
(B) Apo-B
(C) Apo-C
(D) Apo-D
72. The
apolipoprotein which forms the integral component of chylomicron is
(A) B-100
(B) B-48
(C) C
(D) D
73. The
apolipoprotein which from the integral component of VLDL is
(A) B-100
(B) B-48
(C) A
(D) D
74. The
apolipoprotein which acts as ligand for LDL receptor is
(A) B-48
(B) B-100
(C) A
(D) C
75. Serum
LDL has been found to be increased in
(A) Obstructive jaundice
(B) Hepatic
jaundice
(C) Hemolytic
jaundice
(D)
Malabsorption syndrome
76. A lipoprotein
associated with high incidence of coronary atherosclerosis is
(A) LDL
(B) VLDL
(C) IDL
(D) HDL
77. A
lipoprotein inversely related to the incidence of coronary artherosclerosis is
(A) VLDL
(B) IDL
(C) LDL
(D) HDL
78. The
primary biochemical lesion in homozygote with familial hypercholesterolemia
(type IIa) is
(A) Loss of feed back inhibition of HMG reductase
(B) Loss of
apolipoprotein B
(C) Increased production of LDL from VLDL
(D) Functional
deficiency of plasma membrane receptors for LDL
79. In
abetalipoproteinemia, the biochemical defect is in
(A) Apo-B
synthesis
(B) Lipprotein lipase activity
(C) Cholesterol ester hydrolase
(D) LCAT activity
80.
Familial hypertriaacylglycerolemia is associated with
(A) Over
production of VLDL
(B) Increased LDL concentration
(C) Increased HDL concentration
(D) Slow clearance of chylomicrons
81. For
synthesis of prostaglandins, the essential fatty acids give rise to a fatty acid
containing
(A) 12
carbon atoms
(B) 16
carbon atoms
(C) 20 carbon atoms
(D) 24
carbon atoms
82. All
active prostaglandins have at least one double bond between positions
(A) 7 and 8
(B) 10 and
11
(C) 13 and
14
(D) 16 and
17
83. Normal
range of plasma total phospholipids is
(A) 0.2-0.6
mmol/L
(B) 0.9-2.0
mmol/L
(C) 1.8-5.8 mmol/L
(D) 2.8-5.3
mmol/L
84. HDL2
have the density in the range of
(A) 1.006-1.019
(B) 1.019-1.032
(C) 1.032-1.063
(D) 1.063-1.125
85. β-lipoproteins have the density in the range
of
(A) 0.95-1.006
(B) 1.006-1.019
(C) 1.019-1.063
(D) 1.063-1.125
86. IDL
have the density in the range of
(A) 0.95-1.006
(B) 1.006-1.019
(C) 1.019-1.032
(D) 1.032-1.163
87.
Aspirin inhibits the activity of the enzyme:
(A)
Lipoxygenase
(B) Cyclooxygenase
(C)
Phospholipae A1
(D) Phospholipase
A2
88. A
’suicide enzyme’ is
(A) Cycloxygenase
(B)
Lipooxygenase
(C)
Phospholipase A1
(D)
Phospholipase A2
89.
In adipose tissue
prostaglandins decrease
(A) Lipogenesis
(B) Lipolysis
(C)
Gluconeogenesis
(D)
Glycogenolysis
90. The
optimal pH for the enzyme pepsin is
(A) 1.0-2.0
(B) 4.0-5.0
(C) 5.2-
6.0
(D) 5.8-6.2
91.
Pepsinogen is converted to active pepsin by
(A) HCl
(B) Bile salts
(C) Ca++
(D)
Enterokinase
92. The
optimal pH for the enzyme rennin is
(A) 2.0
(B) 4.0
(C) 8.0
(D) 6.0
93. The optimal pH for the enzyme trypsin is
(A) 1.0-2.0
(B) 2.0-4.0
(C) 5.2-6.2
(D) 5.8-6.2
94. The optimal pH for the enzyme chymotrypsin is
(A) 2.0
(B) 4.0
(C) 6.0
(D) 8.0
95. Trypsinogen is converted to active trypsin by
(A) Enterokinase
(B) Bile salts
(C) HCl
(D) Mg++
96. Pepsin acts on denatured proteins to produce
(A) Proteoses and peptones
(B)
Polypeptides
(C) Peptides
(D) Dipeptides
97. Renin
converts casein to paracasein in presence of
(A) Ca++
(B) Mg++
(C) Na+
(D) K+
98. An expopeptidase is
(A) Trypsin
(B)
Chymotrypsin
(C) Elastase
(D) Elastase
99. The
enzyme trypsin is specific for peptide bonds of
(A) Basic amino acids
(B) Acidic
amino acids
(C) Aromatic
amino acids
(D) Next to
small amino acid residues
100.
Chymotrypsin is specific for peptide bonds containing
(A) Uncharged amino acid residues
(B) Acidic
amino acids
(C) Basic amino
acid
(D) Small amino
acid residues
101. The
end product of protein digestion in G.I.T. is
(A) Dipeptide
(B) Tripeptide
(C) Polypeptide
(D) Amino acid
102.
Natural L-isomers of amino acids are absorbed from intestine by
(A) Passive
diffusion
(B) Simple
diffusion
(C) Faciliated
diffusion
(D) Active process
103.
Abnormalities of blood clotting are
(A) Haemophilia
(B) Christmas
disease
(C) Gout
(D) Both (A) and (B)
104. An
important reaction for the synthesis of amino acid from carbohydrate intermediates
is transamination
which requires the cofactor:
(A) Thiamin
(B) Riboflavin
(C) Niacin
(D) Pyridoxal phosphate
105. The
main sites for oxidative deamination are
(A) Liver and kidney
(B) Skin and
pancreas
(C) Intestine
and mammary gland
(D) Lung and
spleen
106. A
positive nitrogen balance occurs
(A) In growing infant
(B) Following
surgery
(C) In advanced
cancer
(D) In
kwashiorkar
107. The
main site of urea synthesis in mammals is
(A) Liver
(B) Skin
(C) Intestine
(D) Kidney
108. The
enzymes of urea synthesis are found in
(A)
Mitochondria only
(B) Cytosol
only
(C) Both mitochondria and cytosol
(D) Nucleus
109. The
number of ATP required for urea synthesis is
(A) 0
(B) 1
(C) 2
(D) 3
110. Most
of the ammonia released from L-α-amino acids reflects the coupled action of transaminase
and
(A) L-glutamate dehydrogenase
(B) L-amino
acid oxidase
(C) Histidase
(D) Serine
dehydratase
111. In
urea synthesis, the amino acid functioning solely as an enzyme activator:
(A) N-acetyl glutamate
(B) Ornithine
(C) Citrulline
(D) Arginine
112. The
enzyme carbamoyl phosphate synthetase requires
(A) Mg++
(B) Ca++
(C) Na+
(D) K+
113.
Control of urea cycle involves the enzyme:
(A) Carbamoyl phosphate synthetase
(B) Ornithine
transcarbamoylase
(C)
Argininosuccinase
(D) Arginase
114.Transfer
of the carbamoyl moiety of carbamoyl phosphate to ornithine is catalysed by a
liver mitochondrial
enzyme:
(A) Carbamoyl
phosphate synthetase
(B) Ornithine transcarbamoylase
(C) N-acetyl
glutamate synthetase
(D) N-acetyl
glutamate hydrolase
115. A
compound serving a link between citric acid cycle and urea cycle is
(A) Malate
(B) Citrate
(C) Succinate
(D) Fumarate
116. The
2 nitrogen atoms in urea are contributed by
(A) Ammonia and
glutamate
(B) Glutamine and glutamate
(C) Ammonia and aspartate
(D) Ammonia and
alanine
117. In
carcinoid syndrome the argentaffin tissue of the abdominal cavity overproduce
(A) Serotonin
(B) Histamine
(C) Tryptamine
(D) Tyrosine
118.
Tryptophan could be considered as precursor of
(A) Melanotonin
(B) Thyroid
hormones
(C) Melanin
(D) Epinephrine
119.
Conversion of tyrosine to dihydroxyphenylalanine is catalysed by tyrosine
hydroxylase which requires
(A) NAD
(B) FAD
(C) ATP
(D) Tetrahydrobiopterin
120. The
rate limiting step in the biosynthesis of catecholamines is
(A)
Decarboxylation of dihydroxyphenylalanine
(B)
Hydroxylation of phenylalanine
(C) Hydroxylation of tyrosine
(D) Oxidation
of dopamine
121. The
enzyme dopamine β-oxidase which catalyses conversion of dopamine to norepinephrine
requires
(A) Vitamin A
(B) Vitamin C
(C) Vitamin E
(D) Vitamin B12
122. In
humans the sulphur of methionine and cysteine is excreted mainly as
(A) Ethereal
sulphate
(B) Inorganic sulphate
(C) Sulphites
(D) Thioorganic
compound
123. Small
amount of urinary oxalates is contributed by the amino acid:
(A) Glycine
(B) Tyrosine
(C) Alanine
(D) Serine
124. The
amino acid which detoxicated benzoic acid to form hippuric acid is
(A) Glycine
(B) Alanine
(C) Serine
(D) Glutamic
acid
125. The
amino acids involved in the synthesis of creatin are
(A) Arginine, glycine, active methionine
(B) Arginine,
alanine, glycine
(C) Glycine,
lysine, methionine
(D) Arginine,
lysine, methionine
126. Chemical
score of egg proteins is considered to be
(A) 100
(B) 60
(C) 50
(D) 40
127.
Chemical score of milk proteins is
(A) 70
(B) 65
(C) 60
(D) 40
128. Chemical
score of proteins of bengal gram is
(A) 70
(B) 60
(C) 44
(D) 42
129.
Chemical score of protein gelatin is
(A) 0
(B) 44
(C) 57
(D) 60
130. Chemical
score of protein zein is
(A) 0
(B) 57
(C) 60
(D) 70
131.
Biological value of egg white protein is
(A) 94
(B) 83
(C) 85
(D) 77
132. Net
protein utilisation of egg protein is
(A) 75%
(B) 80%
(C) 91%
(D) 72%
133. Net
protein utilization of milk protein is
(A) 75%
(B) 80%
(C) 86%
(D) 91%
134. A
limiting amino acid is an essential amino acid
(A) That is most deficient in proteins
(B) That is
most excess in proteins
(C) That which
increases the growth
(D) That which
increases the weight gain
135. The
limiting amino acid of rice is
(A) Lysine
(B) Tryptophan
(C)
Phenylalanine
(D) Tyrosine
136. The
limiting amino acid of fish proteins is
(A) Tryptophan
(B) Cysteine
(C) Lysine
(D) Threonine
137.
Pulses are deficient in
(A) Lysine
(B) Threonine
(C) Methionine
(D) Tryptophan
138. A
trace element deficient in the milk is
(A) Magnesium
(B) Copper
(C) Zinc
(D) Chloride
139. A
conjugated protein present in the egg yolk is
(A) Vitellin
(B) Livetin
(C) Albuminoids
(D) Ovo-mucoid
140. The
chief protein of cow’s milk is
(A) Albumin
(B) Vitellin
(C) Livetin
(D) Casein
141. A
water soluble vitamin deficient in egg is
(A) Thiamin
(B) Ribofalvin
(C) Ascrobic acid
(D) Cobalamin
142. Pulses
are rich in
(A) Lysine
(B) Methionine
(C) Tryptophan
(D)
Phenylalanine
143. Milk
is deficient in
(A) Vitamin B1
(B) Vitamin B2
(C) Sodium
(D) Potassium
144. Milk
is deficient in
(A) Calcium
(B) Iron
(C) Sodium
(D) Potassium
145. When
net protein utilization (NPU) is low, the requirements for proteins are
(A) High
(B) Moderate
(C) Low
(D) Supplementary
146.
Protein content of human milk is about
(A) 1.4%
(B) 2.4%
(C) 3.4%
(D) 4.4%
147.
Protein content of cow’s milk is about
(A) 2.5%
(B) 3.5%
(C) 4.5%
(D) 5.5%
148.
Protein content of soyabean is about
(A) 30%
(B) 40%
(C) 50%
(D) 60%
149.
Lipid content of egg white is
(A) 12%
(B) 33%
(C) 10-11%
(D) Traces
150. The
recommended daily allowance (RDA) of proteins for an adult man is
(A) 70 gms
(B) 50 gms
(C) 40 gms
(D) 30 gms
151. The
basic amino acids are
(A) Lysine
(B) Bile acids
(C) Glycine
(D) Alanine
152. The
daily caloric requirement for the normal adult female is about
(A) 1500
(B) 2100
(C) 2500
(D) 2900
153. In
the total proteins, the percentage of albumin is about
(A) 20-40
(B) 30-45
(C) 50-70
(D) 80-90
154. In
the total proteins percentage of α globulin is about
(A) 0.2-1.2%
(B) 1.2-2.0%
(C) 2.4-4.4%
(D) 5.0-10.0%
155. In
the total proteins the percentage ofγ globulin is about
(A) 2.4-4.4%
(B) 10.0-21.0%
(C) 6.1-10.1%
(D) 1.2-2.0%
156. Most
frequently the normal albumin globulin ratioratio (A : G) is
(A) 1.0 :
0.8
(B) 1.5 :
1.0
(C) 2.0 : 1.0
(D) 2.4 :
1.0
157. In
Thymol turbidity test the protein involved is mainly
(A) Albumin
(B) α1-Globulin
(C) α2-Globulin
(D) β Globulin
158. In
quaternary structure, subunits are linked by
(A) Peptide bonds
(B) Disulphide
bonds
(C) Covalent bonds
(D) Non-covalent bonds
159.
Molecular weight of human albumin is about
(A) 156,000
(B) 90,000
(C) 69,000
(D) 54,000
160. At
isoelectric pH, an amino acid exists as
(A) Anion
(B) Cation
(C) Zwitterion
(D) None of
these
161. A
disulphide bond can be formed between
(A) Two
methionine residues
(B) Two cysteine residues
(C) A
methionine and a cysteine residue
(D) All of
these
162. A
coagulated protein is
(A) Insoluble
(B)
Biologically non-functional
(C) Unfolded
(D) All of the above
163. At a
pH below the isoelectric point, an amino acid exists as
(A) Cation
(B) Anion
(C) Zwitterion
(D)
Undissociated molecule
164. An
amino acid having a hydrophilic side chain is
(A) Alanine
(B) Proline
(C) Methionine
(D) Serine
165. An
amino acid that does not take part in α helix formation is
(A) Histidine
(B) Tyrosine
(C) Proline
(D) Tryptophan
166. A
protein rich in cysteine is
(A) Collagen
(B) Keratin
(C) Haemoglobin
(D) Gelatin
167.
Primary structure of proteins can be determined by the use of
(A) Electrophoresis
(B)
Chromatography
(C) Ninhydrin
(D) Sanger’s reagent
168.
Electrostatic bonds can be formed between the side chains of
(A) Alanine and
leucine
(B) Leucine and
valine
(C) Asparate
and glutamate
(D) Lysine and aspartate
169.
Sanger’s reagent contains
(A)
Phenylisothiocyanate
(B) Dansyl
chloride
(C) 1-Fluoro-2,
4-dinitrobenzene
(D) Ninhydrin
170. The
most abundant protein in mammals is
(A) Albumin
(B) Haemoglobin
(C) Collagen
(D) Elastin
171.
Folding of newly synthesized proteins is accelerated by
(A) Protein
disulphide isomerase
(B) Prolyl
cis-trans isomerise
(C) Chaperonins
(D) All of these
172.
Primary structure of a protein is formed by
(A) Hydrogen
bonds
(B) Peptide bonds
(C) Disulphide
bonds
(D) All of
these
173.
α-Helix is formed by
(A) Hydrogen bonds
(B) Hydrophobic
bonds
(C)
Electrostatic bonds
(D) Disulphide
bonds
174.
Glutelins are present in
(A) Milk
(B) Eggs
(C) Meat
(D) Cereals
175.
Aromatic amino acids can be detected by
(A) Sakaguchi
reaction
(B) Millon-Nasse reaction
(C)
Hopkins-Cole reaction
(D) Xanthoproteic reaction
176. Two
amino groups are present in
(A) Leucine
(B) Glutamate
(C) Lysine
(D) Threonine
177.
During denaturation of proteins, all of the following are disrupted except
(A) Primary
structure
(B) Secondary structure
(C) Tertiary
structure
(D) Quaternary
structure
178. All
the following are branched chain amino acids except
(A) Isoleucine
(B) Alanine
(C) Leucine
(D) Valine
179. An
-OH group is present in the side chain of
(A) Serine
(B) Arginine
(C) Lysine
(D) Proline
180.
Edman’s reagent contains
(A) Phenylisothiocyanate
(B) 1-Fluoro-2, 4-dinitrobenzene
(C) Dansyl
Chloride
(D) tBOC azide
181.
Edman’s reaction can be used to
(A) Determine the
number of tyrosine residues in a protein
(B) Determine
the number of aromatic amino acid residues in a protein
(C) Determine the amino acid sequence of a
protein
(D) Hydrolyse
the peptide bonds in a protein
182.
Inherited deficiency of β−glucosidase causes
(A) Tay-Sachs
disease
(B)
Metachromatic leukodystrophy
(C) Gaucher’s disease
(D) Multiple
sclerosis
183.
Tay-Sachs disease results from inherited deficiency of
(A)
Arylsulphatase A
(B) Hexosaminidase A
(C)
Sphingomyelinase
(D) Ceramidase
184. The
largest alpolipoprotein is
(A) Apo E
(B) Apo B-48
(C) Apo B-100
(D) Apo A-I
185.
Apolipoprotein B-100 is synthesised in
(A) Adipose
tissue
(B) Liver
(C) Intestine
(D) Liver and
intestine
186.
Apolipoprotein B-48 is synthesized in
(A) Adipose
tissue
(B) Liver
(C) Intestine
(D) Liver and
intestine
187.
Apolipoproteins A-I and A-II are present in
(A) LDL only
(B) LDL and
VLDL
(C) HDL only
(D) HDL and chylomicrons
188.
Apolipoprotein B-48 is present in
(A) Chylomicrons
(B) VLDL
(C) LDL
(D) HDL
189.
Apolipoprotein B-100 is present in
(A)
Chylomicrons
(B) VLDL only
(C) LDL only
(D) VLDL and
LDL
190.
Apolipoproteins C-I, C-II and C-III are present in
(A)
Chylomicrons
(B) VLDL
(C) HDL
(D) All of these
191.
Apolipoprotiens C-I, C-II and C-III are present in all of the following except
(A)
Chylomicrons
(B) VLDL
(C) LDL
(D) HDL
192.
Apolipoprotein A-I acts as
(A) Enzyme
activator
(B) Ligand for
receptor
(C) Both (A) and (B)
(D) None of
these
193.
Apolipoprotien B-100 acts as
(A) Enzyme
activator
(B) Ligand for receptor
(C) Both (A)
and (B)
(D) None of
these
194.
Apolipoprotein C-II is an activator of
(A) Lecithin
cholesterola acyl transferase
(B)
Phospholipase C
(C) Extrahepatic lipoprotein lipase
(D) Hepatic
lipoprotein lipase
195.
Nascent chylomicron receives apolipoproteins C and E from
(A) VLDL
remnant
(B) VLDL
(C) LDL
(D) HDL
196.
Terminal transferase
(A) Removes
nucleotides from 3’ end
(B) Adds nucleotides at 3’ end
(C) Removes
nucleotides from 3’end
(D) Adds
nucleotides at 3’end
197. S1
nuclease hydrolyses
(A) DNA of
somatic cells
(B) DNA of
sperms
(C) Any double
stranded DNA
(D) Any single stranded DNA
198.
Positive nitrogen balance is seen in
(A) Starvation
(B) Wasting
diseases
(C) Growing age
(D) Intestinal
malabsorption
199.
Alanine can be synthesized from
(A) Glutamate
and α-ketoglutarate
(B) Pyruvate and glutamate
(C) Pyruvate
and α-ketoglutarate
(D) Asparate
and α-ketoglutarate
200. All
of the following are required for synthesis of alanine except
(A) Pyruvate
(B) α-ketoglutarate
(C) Glutamate
(D) Pyridoxal
phosphate
201. All
of the following statements about aspartate are true except
(A) It is
non-essential amino acid
(B) It is a dicarboxylic amino acid
(C) It can be synthesized from pyruvate and
glutamate
(D) It can be
converted into asparagine
202.
Glycine can be synthesized from
(A) Serine
(B) Choline
(C) Betaine
(D) All of these
203. All
of the following are required for synthesis of glutamine except
(A) Glutamate
(B) Ammonia
(C) Pyridoxal phosphate
(D) ATP
204. A
coenzyme required for the synthesis of glycine from serine is
(A) ATP
(B) Pyridoxal
phosphate
(C) Tetrahydrofolate
(D) NAD
205. All
of the following statements about proline are true except
(A) It is an
imino acid
(B) It can be
synthesized from glutamate
(C) It can be
catabolised to glutamate
(D) Free proline can be hydroxylated to
hydroxyproline
206. A
protein rich in hydroxyproline is
(A) Prolamin
(B) Procollagen
(C) Collagen
(D) Proinsulin
207. All
the following statement about hydroxyproline are true except
(A) There is no
codon for hydroxyproline
(B) It is present in large amounts in
collagen
(C) Free
proline cannot be hydroxylated to hydroxyproline
(D) Hydroxylation of proline residues is
catalysed by a dioxygenase
208. All
of the following are required for hydroxylation of proline residues except
(A) Ascorbic
acid
(B) Glutamate
(C) Ferrous
ions
(D) Molecular
oxygen
209.
Cysteine can be synthesized from methionine and
(A) Serine
(B) Homoserine
(C)
Homocysteine
(D) Threonine
210.
Methionine is synthesized in human body from
(A) Cysteine
and homoserine
(B)
Homocysteine and serine
(C) Cysteine
and serine
(D) None of these
211.
Hydroxylation of phenylalanine requires all of the following except
(A)
Phenylalanine hydroxylase
(B)
Tetrahydrobiopterin
(C) NADH
(D) Molecular
oxygen
212.
Non-Protein amino acids are
(A) Ornithine
(B) β-alanine
(C) γ-amino
butyric acid
(D) All of
these
213. The
amino acid that undergoes oxidative deamination at significant rate is
(A) Alanine
(B) Aspartate
(C) Glutamate
(D) Glutamine
214.
Allosteric inhibitor of glutamate dehydrogenase is
(A) ATP
(B) ADP
(C) AMP
(D) GMP
215.
Allsoteric activator of glutamate dehydrogenase is
(A) ATP
(B) GTP
(C) ADP and GDP
(D) AMP and GMP
216. Free
ammonia is released during
(A) Oxidative
deamination of glutamate
(B) Catabolism
of purines
(C) Catabolism
of pyrimidines
(D) All of these
217. An
organ which is extremely sensitive to ammonia toxicity is
(A) Liver
(B) Brain
(C) Kidney
(D) Heart
218.
Ammonia is transported from muscles to liver mainly in the form of
(A) Free ammonia
(B) Glutamine
(C) Asparagine
(D) Alanine
219. The
major site of urea synthesis is
(A) Brain
(B) Kidneys
(C) Liver
(D) Muscles
220.
Carbamoyl phosphate required for urea synthesis is formed in
(A) Cytosol
(B) Mitochondria
(C) Both (A) and
(B)
(D) None of
these
221.
Cytosolic and mitochondrial carbamoyl phosphate synthetase have the following
similarity:
(A) Both use
ammonia as a substance
(B) Both provide carbamoyl phosphate for
urea synthesis
(C) Both require N-acetylglutamate as an
activator
(D) Both are
allosteric enzymes
222. The
following enzyme of urea cycle is present in cytosol:
(A)
Argininosuccinic acid synthetase
(B)
Argininosuccinase
(C) Arginase
(D) All of these
223. ATP
is required in following reactions of urea cycle:
(A) Synthesis
of carbamoyl phosphate and citrulline
(B) Synthesis
of citrulline and argininosuccinate
(C) Synthesis of argininosuccinate and arginine
(D) Synthesis
of carbamoyl phosphate and argininosuccinate
224.
Daily excretion of nitrogen by an adult man is about
(A) 15-20
mg
(B) 1.5-2
gm
(C) 5-10 gm
(D) 15-20
gm
225.
Maple syrup urine diseases is an inborn error of metabolism of
(A)
Sulphur-containing amino acids
(B) Aromatic
amino acids
(C) Branched chain amino acids
(D) Dicarboxylic
amino acids
226.
Cystinuria results from inability to
(A) Metabolise
cysteine
(B) Convert cystine into cysteine
(C) Incorporate
cysteine into proteins
(D) Reabsorb cystine in renal tubules
227. The
defective enzyme in histidinemia is
(A) Histidine
carboxylase
(B) Histidine
decarboxylase
(C) Histidase
(D) Histidine
oxidase
228. All
the following statements about phenylketonuria are correct except
(A)
Phenylalanine cannot be converted into tyrosine
(B) Urinary
excretion of phenylpyruvate and phenyllactate is increased
(C) It can be
controlled by giving a low phenylalanine diet
(D) It leads to decreased synthesis of thyroid
hormones, catecholamines and melanin
229. All
the following statements about albinism are correct except
(A) Tyrosine hydroxylase
(tyrosinase) is absent or deficient in melanocytes
(B) Skin is
hypopigmented
(C) It results in mental retardation
(D) Eyes are
hypopigmented
230.
Glycine is not required for the formation of
(A) Taurocholic acid
(B) Creatine
(C) Purines
(D) Pyrimidines
231.
Histamine is formed from histidine by
(A) Deamination
(B)
Dehydrogenation
(C) Decarboxylation
(D)
Carboxylation
232. DOPA
is an intermediate in the synthesis of
(A) Thyroid
hormones
(B)
Catecholamines
(C) Melanin
(D) Catecholamines and melanin
233. All
the following statements about pepsin are correct except
(A) It is
smaller than pepsinogen
(B) It is
formed by the action of HCl on its precursor
(C) Its optimum
pH is 1.0-2.0
(D) It hydrolyses the C-terminal and N-terminal
peptide bonds of proteins
234.
Pancreatic juice contains the precursors of all of the following except
(A) Trypsin
(B)
Chymotrypsin
(C)
Carboxypeptidase
(D) Aminopeptidase
235. The
only correct statement about chymotrypsin is
(A) It is
formed from trypsin
(B)
Carboxypeptidase converts trypsin into chymotrypsin
(C) Its optimum pH is around 7
(D) It
hydrolyses peptide bonds involving basic amino acids
236. The
portion of the antigen molecule which is recognized by antibody is known as
(A) Hapten
(B) Epitope
(C) Complement
(D) Variable
region
237. All
the following statements about haptens are true except
(A) They have high molecular weights
(B) They cannot
elicit an immune response by themselves
(C) When
combined with some other large molecule, they can elicit an immune response
(D) Once an
immune response develops, the free hapten can be recognized by the antibody
238.
Antigens and haptens have the following similarity:
(A) They have high molecular weights
(B) They can elicit immune response by themselves
(C) They can elicit an immune response only
inassociation with some other large molecule
(D) Once an immune response develops, free
antigen and free hapten can be recognized by the antibody
239. The
minimum number of polypeptide chains in an immunoglobulin is
(A) Two
(B) Four
(C) Five
(D) Six
240.
Light chains of immunoglobulins are of following types:
(A) Alpha and kappa
(B) Alpha and
gamma
(C) Lambda and delta
(D) Kappa and lambda
241.
Immunoglobulins are classified on the basis of
(A) Type of light chains
(B) Type of heavy chains
(C) Types of light and heavy chains
(D) Molecular
weight
242. The
molecular weight of light chains is
(A) 10,000-15,000
(B) 20,000-25,000
(C) 25,000-50,000
(D) 50,000-75,000
243. The
molecular weight of heavy chains is
(A) 20,000-25,000
(B) 25,000-50,000
(C) 50,000-70,000
(D) 70,000-1,00,000
244.
Secretory component is present in
(A) IgA
(B) IgG
(C) IgM
(D) All of
these
245. The
variable region of light chains is the
(A) N-terminal
quarter
(B) N-terminal half
(C) C-terminal
quarter
(D) C-terminal
half
246. The
variable region of light chain is the
(A) N-terminal quarter
(B) N-terminal
half
(C) C-terminal
quarter
(D) C-terminal
half
247. The
variable region of light chains has
(A) One
hypervariable region
(B) Two hypervariable regions
(C) Three hypervariable regions
(D) Four
hypervariable regions
248. The
variable region of heavy chains has
(A) One
hypervariable region
(B) Two
hypervariable regions
(C) Three
hypervariable regions
(D) Four hypervariable regions
249. The
most abundant immunoglobulin in plasma is
(A) IgA
(B) IgG
(C) IgM
(D) IgD
250. The
largest immunoglobulin is
(A) IgA
(B) IgG
(C) IgM
(D) IgD
251. The
plasma concentration of IgA is
(A) 1-5
mg/dl
(B) 40-200
mg/dl
(C) 60-500 mg/dl
(D) 700-1,500
mg/dl
252. An
immunoglobulin found in exocrine secretions is
(A) IgA
(B) IgG
(C) IgM
(D) IgE
253.
Allergic reactions are mediated by
(A) IgA
(B) IgG
(C) IgD
(D) IgE
254. An
immunoglobulin which can cross the placental barrier is
(A) IgA
(B) IgM
(C) IgD
(D) None of these
255. IgM
possesses
(A) Two light
chains and two heavy chains
(B) Four light chains and four heavy
chains
(C) Six light
chains and six heavy chains
(D) Ten light chains and ten heavy chains
256. The
immunoglobulin having the longest half-life is
(A) IgA
(B) IgG
(C) IgM
(D) IgE
257. The
half-life of IgG is
(A) 2-3
days
(B) 5-6
days
(C) 8-10
days
(D) 20-25 days
258.
Recognition of antigen is the function of
(A) Variable
region of light chains
(B) Variable regions of light and heavy chains
(C) Constant
region of heavy chains
(D) Constant
regions of light and heavy chains
259. The
effector function of antibody is performed by
(A) Variable
region of light chains
(B) Constant region of heavy chains
(C) Variable
regions of light and heavy chains
(D) Constant regions of light and heavy chains
260.
Complement system can be activated by binding of antigen to
(A) IgA
(B) IgD
(C) IgE
(D) IgM
261. C1
component of classical complement pathway is made up of
(A) Complements
1q and 1r
(B) Complements 1q and 1s
(C) Complements
1r and 1s
(D) Complements 1q, 1r and 1s
262. The
components of complement system are activated by
(A) Microsomal
hydroxylation
(B)
Phosphorylation
(C)
Glycosylation
(D) Proteloysis
263. The
component system forms a membrane attack complex made up of
(A) Complements
1q, 1r and 1s
(B) Complements 1, 2, 3 and 4
(C) Complements
5b, 6, 7 and 8
(D) Factors B and D
264.
Factors B and D are required in
(A) The
classical pathway of complement fixation
(B) The alternate complement pathway
(C) Both (A)
and (B)
(D) None of
these
265. The
alternate complement pathway doesn’t involve
(A) Antigen-antibody complex
(B) Complement
3
(C) Factors B
and D
(D) Membrane
attack unit
266.
Antibody diversity arises from
(A) Gene
amplification
(B) Gene re-arrangement
(C) Alternative
splicing
(D) All of
these
267. A
light chain gene is constructed from the following segments:
(A) Variable
and constant segments
(B) Variable, joining and constant segments
(C) Variable,
diversity and constant segments
(D) Variable,
joining, diversity and constant segments
268. In
metabolic point of view, amino acids are classified as
(A) Glycogenic
(B) Ketogenic
(C) Glycogenic
or Ketogenic
(D) All of these
269.
Diversity segments are present in
(A) Light chain
genes
(B) Heavy chain genes
(C) Light and
heavy chain genes
(D) None of
these
270.
Constant segments of heavy chains are of
(A) Five types
(B) Six types
(C) Seven types
(D) Eight types
271.
Gamma heavy chains are of
(A) Two types
(B) Three types
(C) Four types
(D) Five types
272.
Gamma heavy chains are present in
(A) IgA
(B) IgG
(C) IgM
(D) IgD
273.
Heavy chains in IgD are of following type:
(A) Alpha
(B) Gamma
(C) Delta
(D) Epsilon
274. On
exposure to any antigen, the first antibody to be formed is of the following
class:
(A) IgA
(B) IgG
(C) IgM
(D) IgE
275.
Constant segment genes of heavy chains are present in a cluster in which the
first gene on side is
(A) Alpha
(B) Gamma
(C) Delta
(D) None of these
276.
Cell-mediated immunity is the function of
(A) B
lymphocytes
(B) T lymphocytes
(C) Plasma
cells
(D) Basophils
277. The
most abundant T cells are
(A) Cytotoxic T
cells
(B) Helper T cells
(C) Suppressor
T cells
(D) Memory T
cells
278. T
cells can recognise
(A) Free
antigens
(B) Antigens
bound to cells
(C) Antigens
bound to antibodies
(D) Antigens bound to MHC proteins
279. MHC
proteins are unique to
(A) Each cell
(B) Each organ
(C) Each individual
(D) Each
species
280. MHC
class I proteins are present on the surface of
(A) B cells
only
(B) T cells
only
(C) Macrophages
only
(D) All cells
281. MHC
class I proteins, in conjunction with antigens are recognised by
(A) Cytotoxic T cells
(B) Helper T
cells
(C) Suppressor
T cells
(D) Memory T
cells
282. MHC
class II proteins are present on the surface of
(A) All cells
(B) B
lymphocytes only
(C) Macrophages
only
(D) Macrophages and B lymphocytes
283. MHC
Class II proteins, in conjunction with antigens, are recognised by
(A) Cytotoxic T
cells
(B) Helper T cells
(C) Suppressor
T cells
(D) Memory T
cells
284. CD 8
is a transmembrane glycoprotein present in
(A) Cytotoxic T
cells
(B) Helper T
cells
(C) Suppressor T cells
(D) Memory T
cells
285. CD 4
is a transmembrane glycoprotein present in
(A) Cytotoxic T cells
(B) Helper T
cells
(C) Suppressor
T cells
(D) Memory T
cells
286. CD 3
complex and p 56lck proteins are present in
(A) Cytotoxic T
cells
(B) Helper T
cells
(C) Both (A)
and (B)
(D) None of these
287.
Cytotoxic T cells release
(A) Perforins
(B) Interleukins
(C) Colony
stimulating factors
(D) Tumour
necrosis factor
288.
Helper T cells release
(A)
Interleukins
(B) Colony stimulating factors
(C) Tumour
necrosis factor
(D) All of
these
289. MHC
Class III proteins include
(A)
Immunoglobulins
(B) Components
of complement system
(C) T cells
receptors
(D) CD4 and CD8 proteins
290.
Human immunodeficiency virus destroys
(A) Cytotoxic T
cells
(B) Helper T cells
(C) B cells
(D) Plasma
cells
291. In
allergic diseases, the concentration of the following is increased in plasma:
(A) IgA
(B) IgG
(C) IgD
(D) IgE
292. IgE
has a tendency to attach to
(A) Basophils
(B) Mast cells
(C) Both (A) and (B)
(D) None of
these
293.
Reaginic antibody is
(A) IgA
(B) IgG
(C) IgD
(D) IgE
294.
Active immunity can be produced by administration of
(A) Killed
bacteria or viruses
(B) Live
attenuated bacteria or viruses
(C) Toxoids
(D) All of these
295.
Passive immunity can be produced by administration of
(A) Pure
antigens
(B) Immunoglobulins
(C) Toxoids
(D) Killed
bacteria or viruses
296.
Helper T cells release all the following except
(A)
Interleukins
(B) Colony
stimulating factors
(C) Perforins
(D) Tumour
necrosis factor
297. IgG
cleaved by papain into
(A) Two light
and two heavy chains
(B) Two Fab and one Fc
fragments
(C) Two pairs
of one light and one heavy chain each
(D) One Fab
and two Fc fragments
298.
Bence-Jones protein is
(A) An
immunoglobulin
(B) A dimer of heavy chains
(C) A dimer of light chains
(D) A dimer of
one heavy and one light chains
299.
Bence-Jones proteins possess all the following properties except
(A) They are
dimers of light chains
(B) Their amino acids sequences are identical
(C) Their
N-terminal halves have variable amino acid sequences
(D) Their
C-terminal halves have constant amino acid sequences
300. A Zwitterion
is
(A) Positive
ion
(B) Negative
ion
(C) Both (A) and (C)
(D) None of
these
301.
After accounting for SDA, the net gain of energy from 25 gm of proteins is
about
(A) 70 kcal
(B) 100
kcal
(C) 130
kcal
(D) 200
kcal
302. After
accounting for SDA, the net gain of energy from 25 gm of carbohydrates is about
(A) 70 kcal
(B) 95 kcal
(C) 100
kcal
(D) 105
kcal
303.
After accounting for SDA, the net gain of energy from 100 gm of fat is about
(A) 600
kcal
(B) 780 kcal
(C) 900
kcal
(D) 1020
kcal
304. If
proteins, carbohydrates and fats are consumed together:
(A) The total
SDA is the sum of individual SDAs of proteins, carbohydrates and fats
(B) The total
SDA is more than the sum of individual SDAs of proteins, carbohydrates and fats
(C) Carbohydrates and fats lower the SDA of
proteins
(D) Proteins
raise the SDA of carbohydrates and fats
305.
After calculating the energy requirement of a person:
(A) 10% kcal are subtracted on account of SDA
(B) 10% kcal
are added on account of SDA
(C) 20% kcal are subtracted on account of SDA
(D) 20% kcal are subtracted on account of SDA
306. The
recommended energy intake for an adult sedentary Indian man is
(A) 1,900
kcal/day
(B) 2,400 kcal/day
(C) 2,700
kcal/day
(D) 3,000
kcal/day
307. The
recommended energy intake for an adult sedentary Indian woman is
(A) 1,900 kcal/day
(B) 2,200
kcal/day
(C) 2,400
kcal/day
(D) 2,700
kcal/day
308.
During pregnancy, the following should be added to the calculated energy
requirement:
(A) 300 kcal/day
(B) 500
kcal/day
(C) 700
kcal/day
(D) 900
kcal/day
309.
During first six months of lactation, the following increment in energy intake
is recommended:
(A) 200
kcal/day
(B) 300
kcal/day
(C) 550 kcal/day
(D) 1,000
kcal/day
310. The
proximate principles of diet are
(A) Vitamins
and minerals
(B) Proteins
(C)
Carbohydrates and fats
(D) Carbohydrates, fats and proteins
311. The
limiting amino acid in wheat is
(A) Leucine
(B) Lysine
(C) Cysteine
(D) Methionine
312. The
limiting amino acid in pulses is
(A) Leucine
(B) Lysine
(C) Tryptophan
(D) Methionine
313.
Maize is poor in
(A) Lysine
(B) Methionine
(C) Tryptophan
(D) Lysine and tryptophan
314. The
percentage of ingested protein/nitrogen absorbed into blood stream is known as
(A) Net protein
utilisation
(B) Protein efficiency ratio
(C) Digestibility coefficient
(D) Biological
value of protein
315.
Biological value of a protein is
(A) The
percentage of ingested protein/nitrogen absorbed into circulation
(B) The percentage of ingested protein/nitrogen
in the body
(C) The
percentage of ingested protein utilised for protein synthesis in the body
(D) The gain in
body weight (gm) per gm of protein ingested
316. Net
protein utilisation depends upon
(A) Protein
efficiency ratio
(B) Digestibility coefficient
(C)
Digestibility coefficient and protein efficiency ratio
(D) Digestibility coefficient and biological
value
317. The
gain in body weight (gm) per gm of protein ingested is known as
(A) Net protein
utilisation
(B) Protein efficiency ratio
(C)
Digestibility coefficient
(D) Biological
value of protein
318. The
following is considered as reference standard for comparing the nutritional
quality of proteins:
(A) Milk
proteins
(B) Egg proteins
(C) Meat proteins
(D) Fish
proteins
319.
Biological value of egg proteins is about
(A) 70 %
(B) 80 %
(C) 86 %
(D) 94 %
320. The
following has the highest protein efficiency ratio:
(A) Milk
proteins
(B) Egg proteins
(C) Meat
proteins
(D) Fish
proteins
321. The
following has the lowest protein efficiency ratio:
(A) Maize proteins
(B) Wheat
proteins
(C) Milk
proteins
(D) Rice
proteins
322.
Protein content of egg is about
(A) 10%
(B) 13%
(C) 16%
(D) 20%
323.
Protein content of meat is about
(A) 10%
(B) 13%
(C) 16%
(D) 20%
324.
Protein content of rice is about
(A) 7%
(B) 12%
(C) 15%
(D) 20%
325. The
calorific value of wheat is about
(A) 2.5
kcal/gm
(B) 3.5 kcal/gm
(C) 4.5
kcal/gm
(D) 5.5
kcal/gm
326. For
vegetarians, pulses are an important source of
(A)
Carbohydrates
(B) Proteins
(C) Fat
(D) Iron
327. The
amino acids present in pulses can supplement the limiting amino acids of
(A) Cereals
(B) Milk
(C) Fish
(D) Nuts and
beans
328. Milk
is a good source of
(A) Proteins,
calcium and iron
(B) Proteins, calcium and ascorbic acid
(C) Proteins, lactose and retinol
(D) Proteins,
lactose and essential fatty acids
329. Milk
is a good source of all of the following except
(A) Essential
amino acids
(B) Vitamin C
(C) Galactose
(D) Calcium and
phosphorous
330. Milk
is poor in
(A) Cholesterol
(B) Retinol
(C) Calcium
(D) Iron
331. Egg
is rich in all of the following except
(A) Cholesterol
(B) Saturated
fatty acids
(C) Ascorbic acid
(D) Calcium
332. A
phosphoprotein present in egg is
(A) Casein
(B) Albumin
(C) Ovoglobulin
(D) Ovovitellin
333.
Consumption of raw eggs can cause deficiency of
(A) Calcium
(B) Lipoic acid
(C) Biotin
(D) Vitamin A
334. Egg
is poor in
(A) Essential
amino acids
(B) Carbohydrates
(C) Avidin
(D) Biotin
335.
Cholesterol is present in all the following except
(A) Milk
(B) Fish
(C) Egg white
(D) Egg yolk
336. Meat
is rich in all of the following except
(A) Iron
(B) Fluorine
(C) Copper
(D) Zinc
337.
Kwashiorkor occurs when the diet is severely deficient in
(A) Iron
(B) Calories
(C) Proteins
(D) Essential
fatty acids
338. Clinical features of Kwashiorkor include all of
the following except
(A) Mental retardation
(B) Muscle
wasting
(C) Oedema
(D) Anaemia
339.
Kwashiorkor usually occurs in
(A) The post-weaning period
(B) Pregnancy
(C) Lactation
(D) Old age
340.
Marasmus occurs from deficient intake of
(A) Essential
amino acids
(B) Essential fatty acids
(C) Calories
(D) Zinc
341.
Marasmus differs from Kwashiorkor in the which of these following respect
(A) Mental
retardation occurs in kwashiorkor but not in marasmus
(B) Growth is
retarded in kwashiorkor but not in marasmus
(C) Muscle wasting occurs in marasmus but not kwashiorkor
(D) Subcutaneous fat disappears in marasmus but
not in kwashiorkor
342.
Energy reserves of an average well-fed adult man are about
(A) 50,000
kcal
(B) 100,000 kcal
(C) 200,000
kcal
(D) 300,000
kcal
343.
During starvation, the first reserve nutrient to be depleted is
(A) Glycogen
(B) Proteins
(C) Triglycerides
(D) Cholesterol
344.
Synthesis of the following enzymes is increased during starvation.
(A) Digestive enzymes
(B) Gluconeogenic enzymes
(C) Urea cycle
enzymes
(D) Glucokinase
345. In
hypoparathyroidism
(A) Plasma calcium and inorganic phosphorous are low
(B) Plasma calcium and inorganic phosphorous are high
(C) Plasma calcium is low and inorganic phosphorous high
(D) Plasma
calcium is high and inorganic phosphorous low
346. The
number of amino acid residues in calcitonin in
(A) 9
(B) 32
(C) 51
(D) 84
347.
Calcitonin is synthesised in
(A) Parathyroid
glands
(B) Thyroid gland
(C) Pars
intermedia of pituitary
(D) Adrenal
cortex
348.
Plasma calcium is lowered by
(A) Parathormone
(B) Calcitonin
(C) Aldosterone
(D)
Deoxycorticosterone
349. α Cells of Islets of Langerhans secrete
(A) Insulin
(B) Glucagon
(C)
Somatostatin
(D)
Cholecystokinin
350. A/G
ratio is
(A) Strength of
proteins
(B) ratio of serum proteins
(C) ratio of
ceruloplasmin
(D) None of
these
351.
Insulin is made up of
(A) A single
polypeptide chain having 51 amino acid residues
(B) A single
polypeptide chain having 84 amino acid residues
(C) A-chain having 21 and B-chain having 30 amino
acid residues
(D) A-chain
having 30 and B-chain having 21 amino acid residues
352. The
number of amino acid residues in preproinsulin is
(A) 51
(B) 84
(C) 109
(D) 119
353.
Pre-proinsulin contains a signal sequence having
(A) 9 amino
acid residues
(B) 19 amino acid residues
(C) 27
amino acid residues
(D) 33
amino acid residues
354. The
number of intra-chain disulphide bonds in pro-insulin:
(A) One
(B) Two
(C) Three
(D) Four
355.
Pentagastrin is a
(A) Naturally
occurring form of gastrin
(B) Inactive
metabolite of gastrin
(C) Active
metabolite of gastrin
(D) Synthetic form of gastrin
356.
Secretion of gastrin is evoked by
(A) Entry of
food into stomach
(B) Vagal
stimulation
(C) Lower
aliphatic alcohols
(D) All of these
357.
Gastrin stimulates
(A) Gastric
motility
(B) Gastric
secretion
(C) Both (A) and (B)
(D) None of
these
358.
Secretin is made up of
(A) 17
amino acids
(B) 27 amino acids
(C) 37
amino acids
(D) 47
amino acids
359.
Secretin causes all of the following except
(A) Secretion
of pancreatic juice
(B) Secretion
of bile
(C) Inhibition
of gastric secretion
(D) Stimulation of intestinal motility
360. All
of the following statements about cholecystokinin pancreozymin are true except
(A) It is
secreted by mucosa of small intestine
(B) It stimulates secretion of pancreatic
juice rich in enzymes
(C) It
stimulates contraction of gall bladder
(D) It inhibits gastric motility
361. All
of the following statements about pancreatic somatostain are true except
(A) It is
secreted by δ cells of islets of Langerhans
(B) It stimulates the secretion of gastrin
(C) It inhibits
the secretion of secretin
(D) It inhibits
the secretion of cholecystokinin pancreozymin
362.
Histidine is converted into histamine by
(A)
Carboxylation
(B) Decarboxylation
(C) Methylation
(D) Hydroxylation
363.
Histamine is synthesised in
(A) Brain
(B) Mast cells
(C) Basophils
(D) All of these
364.
Histamine causes all the following except
(A) Stimulation
of gastric secretion
(B) Vasoconstriction
(C) Pruritus
(D) Increase in
capillary permeability
365. H2-receptors are blocked by
(A)
Diphenhydramine
(B) Mepayramine
(C) Pyrilamine
(D) Cimetidine
366.
Serotonin is synthesised from
(A) Serine
(B)
Phenylalanine
(C) Tyrosine
(D) Tryptophan
367. All
the following statements about serotonin are true except
(A) It causes vasolidatation
(B) It causes bronchoconstriction
(C) It is
metabolized by monoamine oxidase
(D) Its
metabolite is 5-hydroxyindole acetic acid
368. All
the following statements about angiotensin are true except
(A) Its
precursor is an α2-globulin
(B) Its active form is an octapeptide
(C) It is a vasodilator
(D) It
increases the secretion of aldosterone
369.
Methyl dopa decreases blood pressure by
(A) Inhibiting the synthesis of catecholamines
(B) Antagonising
the action of aldosterone
(C) Stimulating
the release of renin
(D) Inhibiting
the breakdown of angiotensin
370.
Binding of gamma-aminobutyric acid to its receptors in brain increases the
permeability of cell membrane to
(A) Cl-
(B) Na+
(C) K+
(D) Ca++
371.
Binding of acetylcholine to its receptors increases the permeability of cell
membrane to
(A) Ca++
(B) Na+
(C) K+
(D) Na+ and K+
372. All
of the following are glycoproteins except
(A) Collagen
(B) Albumin
(C) Transferrin
(D) IgM
373.
Sialic acids are present in
(A)
Proteoglycans
(B) Glycoproteins
(C) Both (A)
and (B)
(D) None of
these
374.
Hyaluronidase hydrolyses
(A) Hyaluronic
acid
(B) Chondroitin
sulphate
(C) Heparin
(D) Hyaluronic acid and chondroitin sulphate
375. The
most abundant protein in bones is
(A) Collagen type I
(B) Collagen type II
(C) Collagen
type III
(D)
Non-collagen proteins
376. The
most abundant collagen in cartilages is
(A) Type I
(B) Type II
(C) Type III
(D) Type IV
377.
Collagen and elastin have the following similarity:
(A) Both are triple helices
(B) Both have
hydroxyproline residues
(C) Both have
hydrolysine residues
(D) Both are
glycoproteins
378.
Abnormal collagen structure is seen in all of the following except
(A) I-cell
disease
(B) Osteogenesis imperfecta
(C) Menke’s
disease
(D)
Ehlers-Danlos sydrome
379.
I-cell disease results from absence of the following from lysosomal enzymes:
(A) Signal
sequence
(B) Mannose-6-phosphate
(C) Sialic acid
(D) A serine residue
380. In
I-cell disease, lysosomal enzymes
(A) Are not
synthesised
(B) Are inactive
(C) Lack signal
sequence
(D) Cannot
reach lysosomes
381.
Renal glycosuria occurs due to
(A) Increased
filtration of glucose in glomeruli
(B) Increased secretion of glucose by
renal tubular cells
(C) Decreased
reabsorption of glucose by renal tubular
cells
(D) Increased conversion of glycogen into glucose
in tubular cells
382.
Haematuria can occur in
(A) Haemolytic
anaemia
(B) Mismatched
blood transfusion
(C) Yellow
fever
(D) Stone in urinary tract
383.
Haematuria can occur in all of the following except
(A) Acute
glomerulonephritis
(B) Cancer of
urinary tract
(C) Stone in
urinary tract
(D) Mismatched blood transfusion
384.
Chyluria can be detected by addition of the following to the urine:
(A)
Sulphosalicylic acid
(B) Nitric acid
(C) Acetic
anhydride
(D) Chloroform
385.
Normal range of serum urea is
(A) 0.6-1.5
mg/dl
(B) 9-11
mg/dl
(C) 20-45 mg/dl
(D) 60-100
mg/dl
386.
Normal range of serum creatinine is
(A) 0.6-1.5 mg/dl
(B) 9-11
mg/dl
(C) 20-45
mg/dl
(D) 60-100
mg/dl
387.
Standard urea clearance is
(A) 54 ml/min
(B) 75
ml/min
(C) 110
ml/min
(D) 130
ml/min
388.
Maximum urea clearance is
(A) 54
ml/min
(B) 75 ml/min
(C) 110
ml/min
(D) 130
ml/min
389.
Average creatinine clearance in an adult man is about
(A) 54
ml/min
(B) 75
ml/min
(C) 110 ml/min
(D) 130
ml/min
390.
Inulin clearance in an average adult man is about
(A) 54
ml/min
(B) 75
ml/min
(C) 110
ml/min
(D) 130 ml/min
391.
Among the following, a test of tubular
function is
(A) Creatinine
clearance
(B) Inulin
clearance
(C) PAH
clearance
(D) PSP excretion test
392. A
simple way to assess tubular function is to withhold food and water for 12
hours and, then, measure
(A) Serum urea
(B) Serum creatinine
(C) Urine
output in one hour
(D) Specific gravity of urine
393.
Among the following, the most sensitive indicator of glomerular function is
(A) Serum urea
(B) Serum
creatinine
(C) Urea
clearance
(D) Creatinine clearance
394. All
the following statements about inulin are correct except
(A) It is
completely non-toxic
(B) It is
completely filtered by glomeruli
(C) It is not
reabsorbed by tubular cells
(D) It is secreted by tubular cells
395. Non-protein
nitrogenous substances in blood include all of the following except
(A) Urea
(B) Uric acid
(C) Creatinine
(D) Inositol
396.
Non-protein nitrogenous substances in blood are raised in
(A) Starvation
(B) Liver damage
(C) Renal
failure
(D) All of
these
397.
Creatinine clearance is deceased in
(A) Acute
tubular necrosis
(B) Acute glomerulonephritis
(C)
Hypertension
(D) Myopathies
398.
Serum amylase is increased in
(A) Acute
parotitis
(B) Acute pancreatitis
(C) Pancreatic
cancer
(D) All of
these
399.
Maximum rise in serum amylase occurs in
(A) Acute
parotitis
(B) Acute pancreatitis
(C) Chronic
pancreatitis
(D) Pancreatic
cancer
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