Effect of temperature on binding of warfarin by human serum albumin.
The in vitro binding of warfarin by human serum albumin was studied at various temperatures and at pH 7.4 by a frontal gel filtration technique. The results can be best described in terms of a two class-of-binding site model, in which the numbers of primary and secondary sites are constrained to the average values for all experiments (n1 = 1.38 and n2 = 3.73). Analysis of the temperature dependence of the binding yielded the following thermodynamic parameters: deltaH1 =-2.55 kcal/mole, deltaS1=16.1 eu, and deltaF1=-7.34 kcal/mole for the primary binding and deltaH2=-5.08 kcal/mole, deltaS2=-1.10 eu, and deltaF2=4.72 kcal/mole for the secondary binding. Calculations based on these results showed that, for the therapeutic concentration range, warfarin was over 99% bound to albumin present in physiological concentration. These findings are compared and contrasted to binding data in the literature for warfarin and salicylate.
D001665:Binding Sites; D006801:Humans; D066298:In Vitro Techniques; D007700:Kinetics; D008954:Models, Biological; D011485:Protein Binding; D012459:Salicylates / Q000097:blood; D012709:Serum Albumin / Q000378:metabolism*; D013696:Temperature; D013816:Thermodynamics; D014859:Warfarin / Q000097:blood*
D012459:Salicylates; D012709:Serum Albumin; D014859:Warfarin