Characterization of Aplysia carboxypeptidase E

Shailaja Juvvadi, Xuemo Fan, Gregg T. Nagle, Lloyd D. Fricker

Research output: Contribution to journalArticle

8 Scopus citations

Abstract

Carboxypeptidase E (CPE) is involved in the biosynthesis of peptide hormones and neurotransmitters. To determine whether a recently reported Aplysia califonrica 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.

Original languageEnglish (US)
Pages (from-to)195-200
Number of pages6
JournalFEBS Letters
Volume408
Issue number2
DOIs
Publication statusPublished - May 19 1997

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Keywords

  • Carboxypeptidase D
  • Carboxypeptidase E
  • Carboxypeptidase H
  • Enkephalin convertase
  • Peptide processing

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

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