Enkephalin convertase: Purification and characterization of a specific enkephalin-synthesizing carboxypeptidase localized to adrenal chromaffin granules

L. D. Fricker, S. H. Snyder

Research output: Contribution to journalArticlepeer-review

Abstract

A specific carboxypeptidase that converts enkephalin precursors into enkephalin in adrenal chromaffin granule has been purified and characterized. In the adrenal this enzyme, designated enkephalin convertase, is uniquely localized to the chromaffin granules, which contain enkephalin and precursor peptides. Enkephalin convertase is markedly stimulated by CoCl2 and inhibited by EDTA or 1,10-phenanthroline, unlike the lysosomal carboxypeptidase. The purified enzyme has a high affinity for the hexapeptides [Met5]- and [Leu5]enkephalin-Arg6 (51 and 83 μM, respectively) and a somewhat lower affinity for the hexapeptides [Met5]- and [Leu5]enkephalin-Lys6 (195 and 174 μM). Brain enkephalin convertase shows 10-fold regional variations, unlike other carboxypeptidases, which are uniformly distributed. Enkephalin convertase appears to be associated selectively and physiologically with biosynthesis of the enkephalins.

Original languageEnglish (US)
Pages (from-to)3886-3890
Number of pages5
JournalProceedings of the National Academy of Sciences of the United States of America
Volume79
Issue number12 I
DOIs
StatePublished - 1982

ASJC Scopus subject areas

  • General

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