Binding equilibrium of I- to serum albumin with resonance Rayleigh scattering
The binding equilibrium between I- and human serum albumin (HSA) or bovine serum albumin (BSA) has been studied by means of the resonance Rayleigh scattering (RRS) and equilibrium dialysis. It has been found for the first time that RRS and multiple frequency scattering (MFS) are enhanced as the I- binding to the HSA and BSA, but fluorescence quenches. The equilibrium dialysis results suggest that the binding of I- to HSA and BSA fits a phase-distribution model other than Scatchard model, and that the order of magnitude of its phase-distribution constant was found to be 104. It is most probable that Cl- or other anion ions influence the binding of I- by changing the ionic strength in the solution. The dialysis at different pH indicates that the binding mechanism is due to the electrostatic forces between the I- and protonated basic amino-acid residues.
作 者： LIANG Hong SHEN Xingcan JIANG Zhiliang HE Xiwen SHEN Panwen 作者单位： LIANG Hong,SHEN Xingcan,JIANG Zhiliang(Institute of Bioinorganic Chemistry, Chemistry and Life Science College, Guangxi Normal University, Guilin 541004, China)HE Xiwen,SHEN Panwen(Department of Chemistry, Nankai University, Tianjin 300071, China)
刊 名： 中国科学B辑（英文版） EI SCI 英文刊名： SCIENCE IN CHINA (CHEMISTRY) 年，卷(期)： 2000 43(6) 分类号： O6 关键词： serum albumin iodine ion resonance Rayleigh scattering equilibrium dialysis phase distribution