title: [Novel carboxypeptidase for processing of animal nerve tissue enkephalins].
abstract: New carboxypeptidase which catalyzes the C-terminal arginine splitting from hexapeptide (an enkephalin precursor) Tyr-Gly-Gly-Phe-Met-Arg is revealed in the cat nerve tissue. The enzyme is activated by cobalt ions, the pH action optimum being 7.6. A relatively high activity of carboxypeptidase in the hypothalamus, midbrain and medulla oblongata permits supposing that it is the key enzyme of the enkephalin processing in areas of the limbic brain system.
authors.forename: M T
authors.initials: MT
authors.lastname: Gengin
authors.forename: A N
authors.initials: AN
authors.lastname: Vernigora
mesh_terms: D000818:Animals; D002268:Carboxypeptidases / Q000032:analysis*; D002415:Cats; D004745:Enkephalins / Q000378:metabolism*; D006863:Hydrogen-Ion Concentration; D009419:Nerve Tissue Proteins / Q000378:metabolism*
chemical_list: D004745:Enkephalins; D009419:Nerve Tissue Proteins; D002268:Carboxypeptidases
vernacular_title: Novaia karboksipeptidaza protsessinga énkefalinov nervnoĭ tkani zhivotnykh.