Kinetics of irreversible enzyme inhibition by an unstable inhibitor.

ABSTRACT: A mathematical treatment for the general case of enzyme inactivation by an inhibitor that breaks down in solution in a first-order reaction is presented. Cathepsin D was inactivated by fluorescein isothiocyanate with a K(i) of 4.47mum. Kinetic constants were also determined for the inactivation of cathepsin D by 1,1-bis(diazoacetyl)-2-phenylethane, and the inactivation of pepsin C by diazoacetyl-dl-norleucine methyl ester.

SUBMITTER: Rakitzis ET 

PROVIDER: S-EPMC1168119 | biostudies-other | 1974 Aug

REPOSITORIES: biostudies-other