Study on the interaction of Pb2+ and bovine serum albumin by fluorescence

被引：0
|
作者：
Wu, GH [1 ]
Wang, CH
机构：
[1] Anqing Teachers Coll, Dept Chem, Anqing 246003, Peoples R China
[2] Nankai Univ, Coll Chem, Tianjin 300071, Peoples R China
来源：
SPECTROSCOPY AND SPECTRAL ANALYSIS | 2005年 / 25卷 / 02期
关键词：
BSA; fluorescence spectrum; Pb2+;
D O I：
暂无
中图分类号：
O433 [光谱学];
学科分类号：
0703 ; 070302 ;
摘要：
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.
引用
收藏
页码：246 / 248
页数：3
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