Chemical and Pharmaceutical Bulletin · 1968 · 20 citations · 0 references
PharmacyBiochemistryChemistryAnalytical ChemistryBiophysical ChemistryProtein BiochemistryBinding KineticsProtein BindingProtein ChemistryAlbumin AdsorptionBovine Serum AlbuminEquilibrium Binding ConstantPh DependencePhosphate Buffer SystemSerum Protein Binding
Binding of anionic dye 2-(4'-hydroxyphenylazo) benzoic acid (HABA) to bovine serum albumin at pH 7.4 was studied spectrophotometrically. The relationship between albuminbound ratio of HABA and concentration of the unbound dye was expressed by a modified Langmuir-type equation involving a repulsing interaction. The binding becomes more difficult with the increasing bonds. The binding constant and the number of binding sites on albumin were evaluated in 0.05 M phosphate buffer solution and in 0.15 M tris. buffer solution at 25°and 37°.