五氯酚对牛血清白蛋白的荧光猝灭作用  

Fluorescence Quench of Bovine Serum Albumin by Pentachlorophenol

作　　者：于兵川[1] 吴洪特[2] 周培疆[1] 南淑清[1] 陆光汉[3] 宋丰[3] 

机构地区：[1]武汉大学资源与环境科学学院,武汉430079 [2]长江大学化学与环境工程学院,荆州434025 [3]华中师范大学化学学院,武汉430072

出　　处：《环境科学》2006年第5期977-980,共4页Environmental Science

基　　金：国家自然科学基金项目(20177018)

摘　　要：用荧光光谱和紫外吸收光谱法研究了五氯酚对牛血清白蛋白(BSA)的荧光猝灭作用.结果表明,五氯酚可以有规律地使BSA内源荧光猝灭,其猝灭机理可认为是五氯酚与BSA形成复合物的静态猝灭;并获得了不同温度下,五氯酚与BSA作用的结合常数和热力学参数.根据所得结果可推断五氯酚与BSA的作用力为疏水作用力和静电作用力.同时由Forster非辐射能量转移理论计算得出了五氯酚与BSA结合位置的距离.The interaction between pentachlorophenol and bovine serum albumin （BSA） were studied using fluorescence spectra and ultraviolet-visible light absorption spectra. The results show that the fluorescence of BSA was quenched regularly by the pentachlorophenol, the mechanism of the fluorescence quench was investigated. The binding constants and thermodynamic parameters of pentachlorophenol with BSA were obtained at different temperatures. The hydrophobic interaction force and electrostatic force played a main role in the binding of pentachlorophenol with BSA. The distances of binding site between pentachlorophenol and BSA were also obtained according to the theory of Forster＇s non-radiative energy transfer.

关 键 词：五氯酚 牛血清白蛋白(BSA) 相互作用 荧光猝灭 

分 类 号：X131[环境科学与工程—环境科学]