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A simple method for determining kinetic constants of slow, tight-binding inhibition
1National Laboratory of Biomacromolecules, Institute of Biophysics, Academia Sinica, Beijing, China.
Analytical Biochemistry
|September 1, 1993
Abstract:
A general procedure is described for determining the kinetic constants of the slow, tight-binding inhibition of enzyme-catalyzed reactions by analyzing the data of initial and steady-state rate. All unknown parameters can be determined from several simple, sequential calculations. This method is simple and rigorous. It is also applicable to the special case of slow-binding inhibition, where the total concentration of inhibitor is much higher than that of the enzyme.