THE HYDROLYSIS OF L-LEUCYL-β-NAPHTHYLAMIDE BY A PREVIOUSLY UNDESCRIBED ENZYME IN WHEAT GERM

Abstract

An enzyme, not leucine aminopeptidase nor any other known isolated enzyme, present in a wheat germ preparation, was found to hydrolyze L-leucyl-[beta]-napthylamide. It differed from leucine aminopeptidase in its sensitivity to p-chloro-mercuribenzoic acid, iodosobenzoic acid, and sodium lauryl sulphate, its resistance to sodium citrate, its inability to hydrolyze leucyl di-and tripeptides, and its neutral pH optimum. It differed from papain and chymotrypsin in its resistance to the action of diisopropyl-flurophosphate. The available data suggests that this enzyme is essentially a naphthylamidase.