Cholecystokinin octa- and tetrapeptide degradation by synaptic membranes. III. Inactivation of CCK-8 by a phosphoramidon-sensitive endopeptidase.

Abstract:

:Solubilization of rat synaptic membranes by Triton X-100 followed by DEAE-cellulose chromatography allowed the separation of a phosphoramidon-sensitive endopeptidase that cleaved CCK-8. This enzymatic activity revealed similar if not identical to "enkephalinase A." A major cleavage point, at the Trp30-Met31 bond, and a minor one at the Tyr27-Met28 bond were identified in the sequence of CCK-8. Replacements of the Met28 and Met31 residues by Thr and either Leu or Nle respectively, in CCK-9 analogues, did not improve the resistance of these peptides to enzymatic degradation. The regional distribution in rat brain of this CCK-8 cleaving endopeptidase displayed marked variations with the highest activity in striatal membranes; it closely followed that described for "enkephalinase" in mouse brain.

journal_name

Peptides

journal_title

Peptides

authors

Deschodt-Lanckman M,Koulischer D,Przedborski S,Lauwereys M

doi

10.1016/0196-9781(84)90098-6

subject

Has Abstract

pub_date

1984-05-01 00:00:00

pages

649-51

issue

3

eissn

0196-9781

issn

1873-5169

pii

0196-9781(84)90098-6

journal_volume

5

pub_type

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