环境毒理
颜承农,李杨,关中杰,刘义.荧光光谱法研究丙酮与牛血清白蛋白的相互作用特征[J].环境科学学报,2006,26(11):1880-1885
荧光光谱法研究丙酮与牛血清白蛋白的相互作用特征
- Studies on the binding interaction features between acetone and bovine serum albumin by fluorescence spectrophtometry
- 基金项目:国家自然科学基金(No.30170010);湖北省自然科学基金(No.2005ABA067)资助项目
- 颜承农
- 长江大学化学与环境工程学院, 荆州 434023
- 李杨
- 长江大学化学与环境工程学院, 荆州 434023
- 关中杰
- 长江大学化学与环境工程学院, 荆州 434023
- 刘义
- 武汉大学化学与分子科学学院, 武汉 430072
- 摘要:在模拟动物体生理条件和不同温度下,用荧光光谱、三维荧光光谱、同步荧光光谱、紫外可见吸收光谱法等研究了丙酮(ACET)与牛血清白蛋白(BSA)的相互作用,证实了丙酮有很强的猝灭BSA荧光强度的能力.分别用Stern-Volmer方程、Lineweaver-Burk双倒数方程和热力学方程等分析和处理试验数据,得到了它们相互作用的生成常数KLV(平均值为7.073×106L·mol-1)、热力学参数(ΔHθ、ΔGθ和ΔSθ的平均值分别为-3.982kJ·mol-1、-26.51kJ·mol-1和73.31J·K-1)和结合位点数(平均值为1.266)等.这为研究ACET对BSA构象的影响、ACET的毒理效应和生物学效应提供了重要信息.
- Abstract:Under the simulated physiological condition of animal body and different temperatures, the interaction between acetone(ACET) and bovine serum albumin (BSA) was studied by the fluorescence spectroscopy, three-dimensional fluorescence spectrum, synchronous fluorescence spectrum and ultra-violet spectrum. It was shown that this compound has a quite strong ability to quench the fluorescence launching from BSA. The average value of binding constant(KLB:7.073×106 L·mol-1),thermodynamic parameters(ΔHθ:-3.982kJ·mol-1,ΔGθ:-26.51 kJ·mol-1 and ΔSθ:73.31 J·K-1) and amounts of binding sites(1.266) were obtained by analyzing and processing the fluorescence quenching data according to Sterm-Volmer equation,Lineweaver-Burk equation and thermodynamic equation, respectively. It provides an important information for researching the configuration modification of BSA on the action of ACET,the toxicity effects and biological effects of ACET on a living body.
摘要点击次数: 2416 全文下载次数: 5236