Kasper Fisker

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Calcium binding to glycated, penicilloylated, acetylated, and normal defatted human serum albumin as well as to mercapt- and nonmercaptalbumin was studied by equilibrium dialysis of radioactive Ca2+. Binding was quantified by five Scatchard constants [ni = 1, (i = 1-4) and n5 = 10]. Glycation resulted in increased k1- and k2-values and unchanged(More)
Determination of binding constants for multiple binding of a ligand usually results in highly variable figures. We have found that the variations depend mainly upon cooperativity of ligand binding, and that cooperativity is generally absent on binding to human serum albumin. When this is taken into account it becomes possible to obtain binding constants(More)
Multiple binding equilibria of two apparently insoluble ligands, palmitate and stearate, to defatted human serum albumin were studied in a 66 mM sodium phosphate buffer (pH 7.4) at 37 degrees C, by determination of dialytic exchange rates of ligands among identical equilibrium solutions. The experimental data were analysed by a computerised curve fitting(More)
Binding equilibria of warfarin, 3-(alpha-acetonylbenzyl)-4-hydroxycoumarin, and phenprocoumon, 3-(alpha-ethylbenzyl)-4-hydroxycoumarin, to defatted human serum albumin (Kabi Vitrum) were studied by equilibrium dialysis in a 33 mM sodium phosphate buffer (pH 7.4) at 37 degrees C. The binding data were analysed in terms of several acceptable sets of binding(More)
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