【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。更多还原

【Abstract】 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.更多还原