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Characterization of Aplysia carboxypeptidase E.

作者信息

Juvvadi S, Fan X, Nagle G T, Fricker L D

机构信息

Department of Molecular Pharmacology, Albert Einstein College of Medicine, Bronx, NY 10461, USA.

出版信息

FEBS Lett. 1997 May 19;408(2):195-200. doi: 10.1016/s0014-5793(97)00426-2.

Abstract

Carboxypeptidase E (CPE) is involved in the biosynthesis of peptide hormones and neurotransmitters. To determine whether a recently reported Aplysia californica cDNA encodes a CPE-like enzyme, this cDNA was expressed in the baculovirus system. The Aplysia CPE is optimal at pH 5.5-6.5 and is inhibited by chelating agents and by the sulfhydryl reagent p-chloromercuriphenyl sulfonate. The effect of divalent cations and active site-directed inhibitors on enzyme activity are generally similar for Aplysia and rat CPE. Western blot analysis using antisera to the N- and C-terminal regions of the Aplysia CPE show that the Aplysia CPE is present in atrial glands and ovotestis. This Aplysia CPE is purified on a p-aminobenzoyl-Arg Sepharose affinity column under conditions that selectively purify rat CPE. Taken together, these results suggest that the previously cloned cDNA represents a CPE-like enzyme that is expressed in Aplysia tissue.

摘要

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