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In vitro degradation of the C‐terminal octapeptide of cholecystokinin by ‘enkephalinase A’
Author(s) -
Deschodt-Lanckman Monique,
Strosberg A.Donny
Publication year - 1983
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(83)80493-1
Subject(s) - enkephalinase , cholecystokinin , in vitro , chemistry , terminal (telecommunication) , degradation (telecommunications) , thiorphan , biochemistry , enzyme inhibitor , computer science , enkephalin , receptor , telecommunications , opioid
As the C‐terminal octapeptide of cholecystokinin represents a putative neurotransmitter in the central nervous system, the membrane‐bound enzymes involved in its inactivation were investigated. Two aminopeptidases, involved in the cleavage of enkephalins, and a metalloendopeptidase were identified in extracts of solubilized synaptic membranes. The metalloendopeptidase, which cleaves CCK‐8 at the Trp 30 —Met 31 bond, appeared to be indistinguishable from ‘enkephalinase A 1 ’ on the basis of its chromatographic behaviour, sensitivity to inhibitors and relative affinities for Met‐ and Leu‐enkephalins. This finding indicates that CCK‐8 is inactivated in vitro by the same peptidases as enkephalins.