Kinetics of irreversible enzyme inhibition by an unstable inhibitor
- 1 August 1974
- journal article
- Published by Portland Press Ltd. in Biochemical Journal
- Vol. 141 (2) , 601-603
- https://doi.org/10.1042/bj1410601
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 Ki of 4.47μm. 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.Keywords
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