| Cu（Ⅱ）与牛血清白蛋白相互作用的荧光光谱研究 |
| |
| 引用本文： | 袁东,申中兰,朱文彩,许青,田其燕.Cu（Ⅱ）与牛血清白蛋白相互作用的荧光光谱研究[J].山东教育学院学报,2011,26(3):29-32. |
| |
| 作者姓名： | 袁东 申中兰 朱文彩 许青 田其燕 |
| |
| 作者单位： | 1. 齐鲁师范学院化学与化工系,山东济南,250013
2. 山东省产品质量监督检验研究院,山东济南,250100 |
| |
| 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。
|
| 关 键 词： | 牛血清白蛋白 荧光光谱 色氨酸 静态猝灭 |
Fluorescence Spectra Study on Interaetion of Cu(Ⅱ)with Bovine Serum Albumin |
| |
| Yuan Dong,Shen Zhonglan,Zhu Wencai,Xu Qing,Tian Qiyan.Fluorescence Spectra Study on Interaetion of Cu(Ⅱ)with Bovine Serum Albumin[J].Journal of Shandong Education Institute,2011,26(3):29-32. |
| |
| Authors: | Yuan Dong Shen Zhonglan Zhu Wencai Xu Qing Tian Qiyan |
| |
| Institution: | Yuan Dong1 Shen Zhonglan2 Zhu Wencai1 Xu Qing1 Tian Qiyan2(1.Department of Chemistry and Chemical Engineering,Qilu Normal University,Jinan 250013,China,2.Shandong Supervision and Inspection Institute for Product Quality,Jinan 250100,China) |
| |
| Abstract: | 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. |
| |
| Keywords: | BSA Fluorescence spectra Tryptophan Static quenching |
| 本文献已被 CNKI 维普 万方数据 等数据库收录！ |
|
