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

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

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 process...

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Veröffentlicht in:	Biochemical and biophysical research communications 1986-07, Vol.138 (1), p.356-362
Hauptverfasser:	Demmer, W, Brand, K
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Sequence Animals Brain - ultrastructure Chromatography, High Pressure Liquid Endopeptidases - metabolism Endorphins - metabolism Golgi Apparatus - enzymology Hydrogen-Ion Concentration Intracellular Membranes - enzymology Protease Inhibitors - pharmacology Rats Rats, Inbred Strains Substrate Specificity
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Zusammenfassung:	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.
ISSN:	0006-291X