Determination and characterization of succinyl tri-alanine p-nitroanilide hydrolyzing metalloendopeptidase in serum.

M Ishida, M Ogawa, T Mori, T Mega

Index: Enzyme 37(4) , 202-7, (1987)

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Abstract

Serum succinyl (Ala)3-p-nitroanilide hydrolyzing elastase-like activity which elevates in patients with obstructive jaundice, is due to the joint action of two enzymes: first, succinyl (Ala)3-p-nitroanilide is cleaved to succinyl (Ala)2 and Ala-p-nitroanilide by metalloendopeptidase, and then Ala-p-nitroanilide is cleaved to Ala and p-nitroaniline by aminopeptidase. We adopt a new assay method for serum endopeptidase activity using HPLC.