An aminopeptidase from bovine brain which catalyzes the hydrolysis of enkephalin

Abstract

An aminopeptidase from bovine brain which catalyzes the hydrolysis of the tyrosyl1-glycine2 bond of methionine5-enkephalin has been purified to electrophoretic homogeneity. The enzyme also catalyzes the hydrolysis of dipeptides, tripeptides, and amino acid beta-naphthylamides. The enzyme can be inactivated by dialysis against EDTA, and reconstituted with divalent metal ions. Inhibition of the enzyme is observed in the presence of p-chloromercuribenzoate and puromycin, the latter compound not being hydrolyzed by the enzyme. The enzyme is composed of a single polypeptide chain of molecular weight approx. 100,000. The properties of this enzyme are similar to those reported for other brain aminopeptidases active on enkephalin, although distinct differences are observed.