The interaction between bovine serum albumin(BSA)and Vitamin E(VE )was investigated using spectral methods. The experimental results showed that the fluorescence intensity of BSA was quenched when VE was added. The quenching mechanism was a static quenching process. The quenching constants(Ksv)were 2. 41×105L·mol-1and 1. 24×105L·mol-1 respectively,and the binding constants(KA)were 1. 33×104 L·mol-1 and 1. 49×103L·mol-1 respectively,and the binding sites(n)were 0. 77 and 0. 65 at 294K and 310K respectively. The thermodynamic parameters showed that the interaction of VE and BSA was driven mainly by the hydrogen bond and Van der Waals force. It was found that the conformation of BSA had changed in the presence of VE by means of synchronous fluorescence. The effects of metal ions on the interaction of VE with BSA was also discussed.%用光谱法研究了维生素E(VE)与牛血清白蛋白(BSA)的相互作用.实验结果表明:VE能导致BSA的内源荧光猝灭,猝灭机制为静态猝灭.在294K和310K时,荧光猝灭速率常数(Ksv)分别为2.41×105L·mol-1和1.24×105L·mol-1、结合常数(KA)分别为1.33×104 L·mol-1和1.49×103L·mol-1及结合位点数(n)分别为0.77和0.65.通过计算热力学参数可推断VE与BSA之间的主要作用力为氢键和范德华力.同步荧光的结果表明VE的存在改变了牛血清白蛋白的分子构象.讨论了金属离子对维生素E与BSA的相互作用的影响.
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