Influence of ionic strength on the binding of sodium aurothiosulphate to human serum albumin.
The effect of ionic strength on the binding of aurothiosulphate to human serum albumin has been studied at 37 degrees and neutral pH by equilibrium dialysis in unbuffered solutions. The effect of ionic strength is more pronounced on the lower association constants K2-K4 than on the high association constant K1. Furthermore a reduction in the number of lower affinity binding sites is observed at low ionic strength. The main ionic strength dependence on the association constants agrees with the Debye-Hückel theory. The extrapolated values of K1 and the sum of K2 to K4 at zero ionic strength are 7.6 X 10(5) M-1 and 1.1 X 10(5) M-1, respectively. It is shown that the observed changes in pH of the albumin solutions during dialysis contains valuable information of the aurothiosulphate-albumin interaction. A molecular binding mechanism is discussed.
D001665:Binding Sites; D006046:Gold / Q000378:metabolism*; D012971:Gold Sodium Thiosulfate / Q000378:metabolism*; D006801:Humans; D006863:Hydrogen-Ion Concentration; D066298:In Vitro Techniques; D009994:Osmolar Concentration; D011485:Protein Binding; D012709:Serum Albumin / Q000378:metabolism*; D013816:Thermodynamics
D012709:Serum Albumin; D006046:Gold; D012971:Gold Sodium Thiosulfate