荧光法研究Pb^(2+)与牛血清白蛋白的相互作用  

Study on the Interaction of Pb^(2+) and Bovine Serum Albumin byFluorescence

作　　者：吴根华[1] 汪春华[2] 

机构地区：[1]安庆师范学院化学与环境科学学院,安徽安庆246003 [2]南开大学化学学院,天津300071

出　　处：《光谱学与光谱分析》2005年第2期246-248,共3页Spectroscopy and Spectral Analysis

基　　金：国家自然科学基金(2017001);安徽省教育厅自然科学基金(2002kj201)资助课题

摘　　要：在模拟生理条件下,用荧光光谱法研究了Pb2+与牛血清白蛋白(BSA)的相互作用。结果表明BSA分子中色氨酸和酪氨酸残基具有荧光发射性质,以283nm激发BSA,在341nm处有很强的荧光发射。在加入Pb2+后,发现Pb2+BSA强荧光峰的位置不变,但荧光强度随着Pb2+浓度的增大而明显减弱,说明Pb2+对BSA有荧光猝灭现象,猝灭以静态猝灭为主,由SternVolmer方程求得Pb2+表观猝灭常数Kq=95×1012L·mol-1·s-1。Pb2+主要与BSA中的N配位形成2∶1配合物,表观络合常数lgK=1161。The interaction of Pb2+ and bovine serum albumin(BSA) was studied under conditions similar to those in human bodies by fluorescence spectra. The results indicated that tryptophan and tyrosine, which were located in BSA, had a max fluorescence emission peak at 341 nm with an excitation wavelength of 283 mn. It was shown that Pb2+ had a powerful ability to quench the BSA fluorescence with a mechanism of a static process rather than a dynamic one. The apparent quenching constant K, was obtained to be 9.5 X 10(12) L-mol(-1)-s(-1) by Stern-Volmer equation. The apparent complexation constant of Pb-2-BSA is 1gK = 11.61. The nitrogen in BSA could coordinate with lead in Pb-2-BSA.

关 键 词：荧光猝灭 PB^2+ 常数 配位 荧光发射 相互作用 配合物 牛血清白蛋白 荧光法 酪氨酸 

分 类 号：O175[理学—数学] O657[理学—基础数学]