Pancreatic insulinase and its inhibition by the A and B chains and partial hydrolysate of insulin

Abstract

Insulin was destroyed rapidly by insulinase of rabbit pancreatic extract. The activity was enhanced threefold by glutathione, and was inhibited by the sulfhydryl poisons, mercuric chloride, cupric sulfate, and p-chloromercuribenzoate. The insulinase was also strongly inhibited by low concentrations of acid hydrolysate of insulin and by the oxidized forms of the B and the A chains of insulin.