中文摘要：

利用紫外-可见吸收光谱和荧光光谱法,在Tris-HCl缓冲溶液中考查了不同温度下镝（Dy）-L-苯丙氨酸-5-氟尿嘧啶三元配合物与牛血清白蛋白（BSA）之间的相互作用。实验表明,配合物对BSA的内源荧光猝灭为静态猝灭过程,并测定该反应在不同温度下的结合常数KA,且配合物与BSA以物质的量比1∶1结合。根据计算出的热力学参数表明,配合物和BSA之间的作用力主要是静电作用。用同步荧光技术考察了配合物对BSA构象的影响,结合位点接近于酪氨酸残基。

英文摘要：

The interaction between Dy-L-phe-5-fu ternary complex and bovine serum albumin （BSA） was investigated via ultraviolet-visible absorption spectra and fluorescence in tris-HC1 buffer solutions at different temperatures. The results showed that static quenching was involved in adding complexin BSA solution. The complex reacted at a molar ratio of 1 ： 1 and the binding constants （Ks ） were determined. The interaction between complex and BSA was driven mainly by electrostatic interactions according to thermodynamic parame- ters. Respectively, the effect of ternary complexes on the conformation of BSA was obtained using synchronous fluores- cence spectroscopy. The binding site is close to the tyrosine residue.