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In vitro degradation of the C-terminal octapeptide of cholecystokinin by 'enkephalinase A'

par Deschodt Lanckman, Monique ;Strosberg, A.D.
Référence FEBS letters, 152, 1, page (109-113)
Publication Publié, 1983

Article révisé par les pairs

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Résumé :

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 Trp30-Met31 bond, appeared to be indistinguishable from 'enkephalinase A1' 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.