Insulin is now being commercially produced by genetic engineering. Insulin consists of two short polypeptide chains: chain A and chain B, that are linked together by disulphide bonds. Insulin, in mammal is synthesised as a prohormone which contains an extra stretch called the C-peptide. During maturation this
C-peptide is removed. The production of insulin could only have been commercially possible if somehow the maturation process of C-peptide been skipped.
This problem was solved in 1988 by Eli Lilly, an American company which prepared functionable insulin from two DNA sequences corresponding to A and B chains of human insulin and introduced them in plasmids of E.coli to produce insulin chains. In this way, chains A and B were produced separately which was extracted, combined by creating disulfide bonds to get human insulin.