BIO CHEMISTRY MCQs WITH ANSWER

BIO CHEMISTRY MCQs  WITH ANSWER

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 α1 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 of γ 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 isomerase (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