A simple method for determining kinetic constants of slow, tight-binding inhibition.

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.