摘要
利用荧光光谱技术,从分子水平上研究了模拟生理条件下Cu2+与牛血清白蛋白(BSA)的相互作用机理。实验结果表明,Cu2+使得内部疏水区域的色氨酸(Trp)等芳香环氨基酸逐步暴露出来,在荧光光谱中表现为BSA内源荧光的猝灭,猝灭机理主要为静态猝灭。Cu2+与BSA的结合常数为8.73×104,结合比为1:1。
The interaction of Cu2＋ to bovine serum albumin（BSA） has been investigated mainly by fluorescence spectra under simulative physiological conditions.Fluorescence data revealed that the microenvironment of tryptophan（Trp） residues altered.,the quenching mechanism of BSA by Cu2＋ was a static quenching process and the binding constant is 8.73×104 and the number of binding site is 1.
出处
《齐鲁师范学院学报》
2011年第3期29-32,共4页
Journal of Qilu Normal University
