Preferential Solvation of Bovine Serum Albumin in Aqueous Guanidine Hydrochloride

作者：Milton E. Noelken, Serge N. Timasheff · 发表于：Journal of Biological Chemistry · 年份：1967 · DOI：10.1016/s0021-9258(18)99478-0 · 被引用次数：99 · 研究领域：Protein Interaction Studies and Fluorescence Analysis、Surfactants and Colloidal Systems、Liquid Crystal Research Advancements

Bovine serum albumin, in aqueous guanidine hydrochloride, interacts preferentially with the solvent components, as was shown by techniques in which refractometry and light scattering and equilibrium dialysis were used.If constant salt molality after dialysis is taken as the reference state for zero binding, then 0.08 f 0.03 and 0.18 f 0.05 g of salt per g of protein is bound at 3 M and 6 M salt, respectively, with similar values at 4 and 5 M salt.These results indicate that (E)T,,+~ (obtained by measuring the difference in density between a protein solution and its dialysate) is 2 to 3 % less than the value obtained at constant molality of salt.