In vitro degradation of the C‐terminal octapeptide of cholecystokinin by ‘enkephalinase A’

FEBS Letters

Strosberg, A.Donny²  Deschodt-Lanckman, Monique¹ 

[1] Department of Biochemistry and Nutrition, Medical School, University of Brussels, Bld de Waterloo, 115, B-1000 Brussels, Belgium;Laboratory Molecular Immunology, IRBM-CNRS, University Paris VII, 2, Place Jussieu, 75251 Paris, France

关键词: C-Terminal octapeptide of cholecystokinin;    Enkephalin;    Neuropeptidase;    Enkephalinase A;    Metalloendopeptidase;    Solubilized synaptic membrane;    CCK-8;    -7;    -6;    -5;    -4;    respectively C-terminal octa-;    hepta-;    hexa-;    penta-;    tetrapeptide of cholecystokinin;    HPLC;    high pressure (or performance) liquid chromatography;    R t;    retention time;    I 50;    concentration giving half-maximal inhibition;   

DOI  :  10.1016/0014-5793(83)80493-1

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown