[Partial characteristics of the basic phenylmethylsulfonylfluoride-inhibited carboxypeptidase from cat brain].
Cat brain carboxypeptidase releasing C-terminal arginine from the synthetic substrate, dansyl-Phe-Leu-Arg, was partially characterized. The enzyme has a molecular weight of 100-120 kDa, displays the maximal activity at pH 6.0-6.5 and is strongly inhibited by phenylmethanesulfonylfluoride and 4-chloromercuribenzoate, less strongly (by 40%) by iodoacetamide and is not inhibited by N-ethylmaleimide, 2-mercaptoethanol, EDTA, Co2+ and guanidinoethylmercaptosuccinic acid. The Km values for the hydrolysis of dansyl-Phe-Leu-Arg and dansyl-Phe-Ala-Arg by soluble carboxypeptidase are 48 and 96 microM, respectively. By all properties, this carboxypeptidase differs from other known carboxypeptidases. Possible participation of the enzyme in neuropeptide metabolism is discussed.
Vernigora
A N
AN
Nikishin
N N
NN
Gengin
M T
MT
D000595:Amino Acid Sequence; D000818:Animals; D001921:Brain / Q000201:enzymology*; D002268:Carboxypeptidases / Q000037:antagonists & inhibitors* / Q000302:isolation & purification / Q000378:metabolism; D002415:Cats; D002850:Chromatography, Gel; D006868:Hydrolysis; D008969:Molecular Sequence Data; D011480:Protease Inhibitors / Q000494:pharmacology*; D013450:Sulfones / Q000494:pharmacology*
D011480:Protease Inhibitors; D013450:Sulfones; C056032:phenylsulfonylfluoride; D002268:Carboxypeptidases