An Aminopeptidase from Bovine Brain Which Catalyzes the Hydrolysis of Enkephalin

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 di‐peptides, tripeptides, and amino acid β‐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 hydro‐lyzed 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. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Journal of Neurochemistry Wiley

An Aminopeptidase from Bovine Brain Which Catalyzes the Hydrolysis of Enkephalin

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Publisher
Wiley
Copyright
Copyright © 1981 Wiley Subscription Services, Inc., A Wiley Company
ISSN
0022-3042
eISSN
1471-4159
DOI
10.1111/j.1471-4159.1981.tb02392.x
Publisher site
See Article on Publisher Site

Abstract

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 di‐peptides, tripeptides, and amino acid β‐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 hydro‐lyzed 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.

Journal

Journal of NeurochemistryWiley

Published: Jan 1, 1981

References

  • A fluorometric assay for choline acetyltransferase and its use in the purification of the enzyme from human placenta
    Hersh, Hersh; Coe, Coe; Casey, Casey

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