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  • Title: An aminopeptidase from bovine brain which catalyzes the hydrolysis of enkephalin.
    Author: Hersh LB, McKelvy JF.
    Journal: J Neurochem; 1981 Jan; 36(1):171-8. PubMed ID: 6780659.
    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.
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