Characterization of an intracellular inhibitor of the carboxypeptidase R from Rhodotorula glutinis.
A peptidic inhibitor of the carboxypeptidase R from Rhodotorula glutinis has been identified and partially purified. A molecular weight of 31 000 was found by gel filtration. The inhibitor is reversibly separated from the carboxypeptidase by chaotropic agents. Removal of the inhibitor by an acid protease explains the osberved activation of the carboxypeptidase by incubation at acidic pH values.
D002268:Carboxypeptidases / Q000037:antagonists & inhibitors*; D006146:Guanidines / Q000494:pharmacology; D007700:Kinetics; D003904:Mitosporic Fungi / Q000201:enzymology*; D008970:Molecular Weight; D010455:Peptides / Q000302:isolation & purification / Q000502:physiology*; D012248:Rhodotorula / Q000201:enzymology*; D013861:Thiocyanates / Q000494:pharmacology
D006146:Guanidines; D010455:Peptides; D013861:Thiocyanates; D002268:Carboxypeptidases