title: A simple method for determining kinetic constants of slow, tight-binding inhibition.
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.
authors.affiliation: National Laboratory of Biomacromolecules, Institute of Biophysics, Academia Sinica, Beijing, China.
authors.forename: Z X
authors.initials: ZX
authors.lastname: Wang
mesh_terms: D004791:Enzyme Inhibitors / Q000493:pharmacokinetics*; D004798:Enzymes / Q000378:metabolism*; D007700:Kinetics; D008432:Mathematical Computing; D011485:Protein Binding
chemical_list: D004791:Enzyme Inhibitors; D004798:Enzymes