Relationship between the inhibition constant (K1) and the concentration of inhibitor which causes 50 per cent inhibition (I50) of an enzymatic reaction.
暂无分享,去创建一个
[1] W. Prusoff,et al. Kinetic and photochemical studies of 3-N-methyl-5-iodo-2-'-deoxyuridine. Sensitization of ultraviolet inactivation of thymidine kinase by 3-N-methyl-5-iodo-2'-deoxyuridine and other halogenated analogs of thymidine. , 1972, The Journal of biological chemistry.
[2] Raymond L. Blakley. The biochemistry of folic acid and related pteridines , 1969 .
[3] S. Cha. A simple method for derivation of rate equations for enzyme-catalyzed reactions under the rapid equilibrium assumption or combined assumptions of equilibrium and steady state. , 1968, The Journal of biological chemistry.
[4] A. Burger. Design of Active-Site-Directed Irreversible Enzyme Inhibitors. , 1967 .
[5] R. Parks,et al. Erythrocytic nucleoside diphosphokinase. II. Isolation and kinetics. , 1966, The Journal of biological chemistry.
[6] John Leyden. Webb,et al. Enzyme and metabolic inhibitors , 1963 .
[7] W. Cleland,et al. The kinetics of enzyme-catalyzed reactions with two or more substrates or products. III. Prediction of initial velocity and inhibition patterns by inspection. , 1963, Biochimica et biophysica acta.
[8] W. Cleland,et al. The kinetics of enzyme-catalyzed reactions with two or more substrates or products. II. Inhibition: nomenclature and theory. , 1963, Biochimica et biophysica acta.
[9] W. Cleland. The kinetics of enzyme-catalyzed reactions with two or more substrates or products. I. Nomenclature and rate equations. , 1963, Biochimica et biophysica acta.