Synthesis of insulin

Human insulin is essential in treating human diabetes mellitus. In the past porcine insulin is used for treatment being the one nearest to human insulin in structure. But it as the unfortunate side effect of developing antibodies and therefore tolerance. It is best to use human insulin and until recently that was impossible. With the use of recombinant DNA human insulin can now be synthesized in the laboratory using eukaryotic or prokaryotic translational vectors.

Insulin is made up of 2 chains held together by disulphide bonds (A & B chains)

The genes for A and B chains are obtained and cloned separately and the plasmid pBR-322 is now attached to lac operon together with insulin gene A or B. After expression cyanogen bromide is used to break the bond between peptide and β- galactosidase, thereby freeing each peptide. The two peptides are now available for coupling. They are joined together by sulphonation and air oxidation and then marketed as human insulin which does not produce antibodies. Its most common trade mark is Humulin.

 

 

 

 

 

 

 

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