| 荧光光谱法研究Hg（Ⅱ）与牛血清白蛋白的相互作用 |
| |
| 引用本文： | 韩木先,邹欣平,李跃勤.荧光光谱法研究Hg（Ⅱ）与牛血清白蛋白的相互作用[J].光谱实验室,2009,26(2):173-176. |
| |
| 作者姓名： | 韩木先 邹欣平 李跃勤 |
| |
| 作者单位： | 湖北师范学院化学与环境工程学院,湖北省黄石市磁湖路82号,435002 |
| |
| 基金项目： | 湖北师范学院研究生启动基金 |
| |
| 摘 要： | 在pH为7.15、离子强度为0.15mol/L的NaCl溶液条件下,采用荧光光谱法研究了Hg（Ⅱ）与牛血清白蛋白的相互作用。实验结果表明,Hg（Ⅱ）对牛血清白蛋白的荧光强度猝灭机理是一种静态猝灭,且Hg2＋与牛血清白蛋白结合的位点数为2,表观络合常数（K）为2.468×10^10L^2·mol^-2。
|
| 关 键 词： | 荧光光谱法 牛血清白蛋白 Hg(Ⅱ) |
Research on the Interaction between Hg(Ⅱ) and Bovine Serum Albumin by Fluorescence Spectroscopy |
| |
| HAN Mu-Xian,ZOU Xin-Ping,LI Yue-Qin.Research on the Interaction between Hg(Ⅱ) and Bovine Serum Albumin by Fluorescence Spectroscopy[J].Chinese Journal of Spectroscopy Laboratory,2009,26(2):173-176. |
| |
| Authors: | HAN Mu-Xian ZOU Xin-Ping LI Yue-Qin |
| |
| Institution: | College of Chemistry and Environmental Engineering;Hubei Normal University;Huangshi;Hubei 435002;P.R China |
| |
| Abstract: | The interaction between Hg（Ⅱ） and Bovine Serum Albumin （BSA） was investigated by Fluorescence Spectroscopy in pH=7.15 buffer solution and ionic strength of 0.15mol/L sodium chloride solution.It was proved that static quenching exits between Hg（Ⅱ） and BSA. The results showed that the number of binding sites is n=2 and the combination constant is K=2.468×10^10L^2·mol^-2. |
| |
| Keywords: | Fluorescence Spectroscopy Bovine Serum Albumin Hg（Ⅱ） |
| 本文献已被 CNKI 维普 万方数据 等数据库收录！ |
