摘要
用荧光光谱、同步荧光光谱和紫外吸收光谱研究了牛血清白蛋白与酚藏花红的结合反应特征。在不同的pH条件下,酚藏花红与蛋白质的反应导致了蛋白质荧光猝灭及酚藏花红的荧光增强,其荧光猝灭值与酚藏花红的浓度成正比,可用于酚藏花红的分析测定;而酚藏花红荧光增强值与蛋白质浓度成正比,又可用于蛋白质的分析测定。用Stern-Volmer方程和Lineweaver-Burk双倒数函数处理实验数据,得到10℃和20℃时动态猝灭常数和静态猝灭结合常数、反应的热力学参数和结合位点数。根据F彲ster能量转移原理计算出20℃时酚藏花红与牛血清白蛋白的结合距离为r=2.22 nm。
The binding feature of phenosafranine（PS） to bovine serum albumins（BSA） was studied by fluorescence speetrophotometry, synchronous fluorescence speetrophotometry and ultraviolet speetrophotometry. A method for the determination of BSA based on the quenching of BSA fluorescence on adding PS and a method for the determination of PS based on the enhancement of PS on adding BSA were developed. The experimental data were processed by the Stern - Volmer equation and Lineweaver - Burk double reciprocal equation. The dynamic quenching constants, the static quenching binding constant, the binding sites number and the basic thermodynamic parameters of the binding process at 10 ℃ and 20 ℃were then obtained. The binding distance （ r = 2.22 nm） between PS and BSA at 20 ℃ was ealculated according to the Foester energy transfer theory.
出处
《分析测试学报》
CAS
CSCD
北大核心
2007年第3期360-364,共5页
Journal of Instrumental Analysis
基金
重庆市教委科研项目(KJ051303)
关键词
酚藏花红
牛血清白蛋白
荧光猝灭
Phenosafranine
Bovine serum albumins
Fluorescence quenching
