Kinetics of irreversible enzyme inhibition by an unstable inhibitor
Keyword(s):
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.
1992 ◽
Vol 57
(7)
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pp. 1451-1458
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2007 ◽
Vol 275
(3)
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pp. 555-562
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1995 ◽
Vol 242
(1-2)
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pp. 228-231
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2008 ◽
Vol 15
(01n02)
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pp. 145-151
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Keyword(s):
1956 ◽
Vol 34
(1)
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pp. 80-82
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