Aa. Saboury et Aa. Moosavimovahedi, A SIMPLE NOVEL METHOD FOR DETERMINATION OF AN INHIBITION CONSTANT BY ISOTHERMAL TITRATION MICROCALORIMETRY - THE EFFECT OF FLUORIDE-ION ON UREASE, Journal of enzyme inhibition, 12(4), 1997, pp. 273-279
A simple novel method was introduced for determination of an inhibitor
binding constant (K-i) and enthalpy of binding by isothermal titratio
n microcalorimetry technique. This method was applied to the binding o
f fluoride ion, as an inhibitor, with the active sites of jack bran ur
ease at pH = 7.0 (Tris 30 mM) and T = 300 degrees K. The dissociation
equilibrium constant measured by this method was markedly consistent w
ith the inhibition constant obtained from assay of enzyme activity in
the presence of fluoride ion.