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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。
Dysprosium (Dy) -L-phenylalanine-5-fluorouracil ternary complex with bovine serum albumin (BSA) was investigated in Tris-HCl buffer solution by UV-Vis absorption spectroscopy and fluorescence spectroscopy interaction between. Experiments show that the quenching of endogenous fluorescence of BSA by the complex is a static quenching process, and the binding constant KA of the reaction at different temperatures is determined. The binding ratio of the complex to BSA is 1: 1. According to the calculated thermodynamic parameters, the interaction between the complex and BSA is mainly electrostatic. The effect of the complex on the conformation of BSA was investigated by synchronous fluorescence technique. The binding site was close to the tyrosine residue.