Characterization of Aplysia carboxypeptidase E

FEBS Letters

Nagle, Gregg T.¹  Fan, Xuemo¹  Fricker, Lloyd D.²  Juvvadi, Shailaja² 

[1] Marine Biomedical Institute and Department of Anatomy and Neurosciences, University of Texas Medical Branch, Galveston, TX 77555, USA;Department of Molecular Pharmacology, Albert Einstein College of Medicine, 1300 Morris Park Avenue, Bronx, NY 10461, USA

关键词: Peptide processing;    Carboxypeptidase E;    Carboxypeptidase H;    Carboxypeptidase D;    Enkephalin convertase;   

DOI  :  10.1016/S0014-5793(97)00426-2

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown