title: Competitive interactions of drugs with their targets: a computerized improvement of Dixon's algorithm.
abstract: Many drugs are competitive and reversible enzyme inhibitors. When the target enzyme kinetics follows the Michaelis-Menten equation, the enzyme affinity of the inhibitor is characterized by a single parameter: the Ki value. This parameter is usually determined via Dixon's procedure: (i). the rate of reaction (V) is measured in the presence of a few concentrations of the inhibitor (I); (ii.) 1/V versus I gives a straight line, which allows a graphic determination of the inhibitory constants, or better via a least-square fit the linear regression. The introduction of appropriate weighting factors in the linear regression may improve the accuracy of the Ki determinations.
authors.affiliation: Muséum d'Histoire Naturelle, URA 401 CNRS, Paris, France.
authors.forename: D
authors.initials: D
authors.lastname: Mattioni
authors.forename: M
authors.initials: M
authors.lastname: Cheminant
authors.forename: R
authors.initials: R
authors.lastname: Labia
mesh_terms: D000465:Algorithms; D001667:Binding, Competitive; D004347:Drug Interactions; D004791:Enzyme Inhibitors / Q000493:pharmacokinetics*; D012044:Regression Analysis
chemical_list: D004791:Enzyme Inhibitors