荧光光谱法研究黄豆黄素与牛血清白蛋白的相互作用  

Study on the Interaction Between Glycitein and BSA by Fluorescence Spectroscopy

作　　者：宋胜梅[1,2] 李艺敏[1] 徐茂田[1] 屈凌波[2] 

机构地区：[1]商丘师范学院化学系河南省高校重点实验室培育基地,河南省商丘市文化路298号476000 [2]郑州大学化学系,郑州市450001

出　　处：《光谱实验室》2011年第2期618-622,共5页Chinese Journal of Spectroscopy Laboratory

基　　金：国家自然科学基金(20775047)

摘　　要：用荧光光谱法在pH 7.4的PBS中研究了黄豆黄素(Glycitein,GL)与牛血清白蛋白(Bovineserum albumin,BSA)分子之间的相互作用方式及机理。结果表明GL可静态猝灭BSA的内源荧光。310K和315K的结合位点数与表观结合常数分别为1.30,8.09×104L.mol-1和1.73,5.22×104L.mol-1。热力学参数表明二者之间的作用力主要是氢键和范德华力。同步荧光光谱表明GL使BSA的结构发生了变化。本研究对于阐明GL与蛋白的相互作用机理具有借鉴意义。The interaction mechanism and mode of glycitein（GL）with bovine serum albumin（BSA） in pH 7.4 PBS was studied by fluorescence spectroscopy.The intrinsic fluorescence of BSA could be quenched by GL.Further more,the numbers of binding site were 1.30 and 1.73 while the apparent binding constants were 8.09×104L·mol-1 and 5.22×104L·mol-1 at 310K and 315K,respectively.The thermodynamic parameters had indicated that the type of force was hydrogen bonding and Van-der Waals force.Synchronous fluorescence spectra showed that the structure of BSA was changed when GL was added.The method could be significant for understanding the interaction mechanism between GL and proteins.

关 键 词：黄豆黄素 牛血清白蛋白 荧光光谱 相互作用 

分 类 号：O657.32[理学—分析化学]