A quick method for the determination of inhibition constants.
The inhibition constant Ki in the common case of competitive inhibition can be obtained by simple comparison of progress curves in the presence and in the absence of inhibitor. The difference between the times taken for the concentration of substrate to fall to the same value is used to obtain Ki. The procedure to use when the product inhibits is described. When there is mixed inhibition, reactions at different substrate concentrations are used to obtain both inhibition constants.
6 references, click to expand
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Enzymic parameters: measurement of V and Km.Biochim Biophys Acta. 1971 Sep 22;242(3):519-22 PMID: 5161034
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Kinetic analysis of progress curves.Methods Enzymol. 1979;63:159-83 PMID: 502859
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Half-time analysis of the integrated Michaelis equation. Simulation and use of the half-time plot and its direct linear variant in the analysis of some alpha-chymotrypsin, papain- and fumarase-catalysed reactions.Biochem J. 1982 May 1;203(2):351-60 PMID: 7115291
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