A putative opioid-peptide processing activity in enriched Golgi fraction from rat brain.

Abstract:

:A Golgi enriched fraction from rat brain was prepared. The preparation has no carboxypeptidase activity and is not contaminated with cytosol, mitochondria and lysosomes as judged by marker enzyme activities for these constituents. Associated with the Golgi membranes a putative opioid peptide processing activity was demonstrated, which acts on Dynorphin 1-13, alpha- and beta-Neoendorphin. The enzyme cleaves the bond between the paired basic residues, releasing Leucine-enkephalin-Arg6. The activity has a pH-optimum around 9 and is inhibited by serine-protease inhibitors. Intracellular location and substrate specificity suggest that this endopeptidase activity may be involved in proenkephalin processing.

authors

Demmer W,Brand K

doi

10.1016/0006-291x(86)90288-3

subject

Has Abstract

pub_date

1986-07-16 00:00:00

pages

356-62

issue

1

eissn

0006-291X

issn

1090-2104

pii

0006-291X(86)90288-3

journal_volume

138

pub_type

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