Biology Questions and Answers – Biotechnological Applications in Medicine: Genetically Engineered Insulin

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This set of Biology Multiple Choice Questions & Answers (MCQs) focuses on “Biotechnological Applications in Medicine: Genetically Engineered Insulin”.

1. How many recombinant therapeutics have been approved for humans to date?
a) 30
b) 20
c) 13
d) 25
View Answer

Answer: a
Explanation: Recombinant therapeutics is the type of medicines obtained from recombinant organisms. These are mostly protein in nature. Till date, 30 recombinant therapeutics have been approved for human use which includes insulin, human factor IX, etc.
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2. Out of 30 how many recombinant therapeutics have been marketed in India?
a) 10
b) 12
c) 30
d) 14
View Answer

Answer: b
Explanation: Out of 30 how many recombinant therapeutics 12 have been marketed in India. These products have been approved by the Genetic Engineering Appraisal Committee (GEAC). Few examples of approved products are Human growth hormone, Human insulin, Erythropoietin, etc.

3. From which animals were insulin obtained in the early days?
a) Insects
b) Lizard and snakes
c) Cats and dogs
d) Cattle and pigs
View Answer

Answer: d
Explanation: In early days the insulin was obtained from the pancreas of cattle and pigs. Insulin obtained this way had many disadvantages. Nowadays insulin is obtained using recombinant DNA technology. For this microorganisms are used.
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4. How many polypeptide chains does insulin consist of?
a) 4
b) 3
c) 2
d) 1
View Answer

Answer: c
Explanation: Insulin consists of two polypeptide chains. These are known as A chain and B chain. A chain is made up of 21 amino acids while the B chain is made up of 30 amino acids. Thus, making insulin a polypeptide containing 51 amino acids.

5. The polypeptide chains present in insulin is connected by _______ bonds.
a) ionic
b) covalent
c) disulphide
d) hydrophobic interactions
View Answer

Answer: c
Explanation: The polypeptide chains present in insulin is connected by disulphide bonds. These disulphide bonds are formed between two cysteine residues. In total insulin consists of 3 disulphide bonds.
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6. Which organ secretes insulin?
a) Stomach
b) Pancreas
c) Thyroid
d) Intestine
View Answer

Answer: b
Explanation: Insulin is secreted by the pancreas. The stomach secretes various digestive enzymes like pepsin and gastric juice. The thyroid secretes thyroid hormones while small intestine secretes trypsin.

7. In mammals insulin is secreted as __________
a) enzyme
b) lipid
c) RNA
d) pro-hormone
View Answer

Answer: d
Explanation: Insulin is a pro-hormone secreted in mammals by the pancreas. This pro-hormone need to be processed to become a fully mature and functional hormone. Insulin allows the absorption of glucose I blood.
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8. Insulin in pro-hormone form contains an extra stretch called _______
a) B-peptide
b) G-peptide
c) C-peptide
d) S-peptide
View Answer

Answer: c
Explanation: The pro-hormone form of insulin consists of an extra stretch called C-peptide. The C peptide is a connecting peptide having approximately 31 amino acids. It connects A and B chain of pro-insulin.

9. _________ is absent in the mature insulin.
a) Lipid
b) A-peptide
c) C-peptide
d) Sequence
View Answer

Answer: c
Explanation: C-peptide is absent in mature insulin. This connecting peptide connects A and B chain in pro-insulin. It is removed during the maturation of pro-insulin to insulin.
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10. ______ in 1983 used recombinant DNA technology to produce insulin.
a) Eli Lilly
b) Emily Lilly
c) Lilly Rose
d) Amy Sanger
View Answer

Answer: a
Explanation: In 1983 Lilly Company of America that was founded by Eli Lilly used recombinant DNA technology to produce insulin. This insulin was obtained from a microorganism.

11. ______ organism was used to produce recombinant insulin.
a) Cyanobacteria
b) E.coli
c) Saccharomyces cerevisiae
d) B. subtilis
View Answer

Answer: b
Explanation: The first recombinant insulin was constructed by using E.coli. It was developed by Lilly Company. E.coli was used because it has a large circular plasmid that can act as a vector, requires less growth time and can be easily grown in a laboratory.

12. C-peptide is removed during ______ phase of insulin.
a) initiation
b) maturation
c) termination
d) elongation
View Answer

Answer: b
Explanation: C-peptide is removed during the maturation phase of insulin production. C-peptide consists of 30 amino acids and it joins two insulin polypeptide chains in pro-insulin. It is released as a by-product of insulin formation.

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