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In 1983, Eli Lilly successfully produced the A and B chains of human insulin separately in genetically engineered E. coli. How were these extracted chains processed to form functionally active mature human insulin?

Options

  1. ABy enzymatically cleaving the C-peptide from the chains
  2. BBy linking the A and B chains using hydrogen bonds
  3. CBy combining them artificially by creating disulfide bonds
  4. DBy introducing human pancreatic enzymes into the bacterial culture to fold them

Correct answer

C. By combining them artificially by creating disulfide bonds

Step-by-step solution

According to NCERT, Eli Lilly prepared two DNA sequences corresponding to A and B chains of human insulin and introduced them in plasmids of E. coli to produce insulin chains. Chains A and B were produced separately, extracted and combined by creating disulfide bonds to form human insulin. Cleaving the C-peptide is a step in the natural maturation of proinsulin in the human body, not in the recombinant process where A and B chains are produced separately. The bonds that link the two chains are disulfide bonds, not

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