中文摘要：

用紫外、荧光、圆二色光谱法研究了氨基黑10B与牛血清白蛋白（BSA）结合反应的光谱特性.结果表明氨基黑10B对牛血清白蛋白的荧光有猝灭作用,其猝灭类型属于静态猝灭;得到了不同温度下的结合常数和结合位点数;利用Gibbs-Helmholtz方程计算得到该猝灭反应的热力学参数,表明氨基黑10B主要以氢键和范德华力与BSA相互作用;圆二色和同步荧光光谱显示氨基黑10B对BSA构象产生了影响.

英文摘要：

The interaction between Amido Black 10B（AB） and Bovine Serum Albumin（BSA） in aqueous solution was studied by UV-vis,fluorescence,and circular dichroism spectroscopy.The intrinsic fluorescence of BSA was quenched by Amido Black 10B,which was explained in terms of the ststics quenching mechanism.The number of binding sites and the apparent binding constants at different temperatures were obtained from Stern-volmer analysis of the fluorescence quenching date.The thermodynamic parameters determined by the Van＇t Hoff analysis of the binding constants（ΔH=-193.466 kJ,ΔS=-540.734 J·mol-1·K-1） clearly indicate that the hydrogen bond and Vander waals force are the main binding forces.Synchronous fluorescence spectroscopy and FT-IR spectra showed the conformation of BSA changed in the presence of AB.