对硝基苯胺与牛血清白蛋白的相互作用  

Interaction of p-Nitroaniline and Bovine Serum Albumin

作　　者：黄芳 周宏[1] 陈昌云[1] 

机构地区：[1]南京晓庄学院生物化工与环境工程学院

出　　处：《光谱实验室》2013年第5期2055-2058,共4页Chinese Journal of Spectroscopy Laboratory

基　　金：国家自然科学基金项目(21171097);南京晓庄学院科研项目(2012NXY18)资助

摘　　要：采用荧光光谱法研究了不同酸度下对硝基苯胺与牛血清白蛋白(BSA)间的相互作用。实验结果表明,对硝基苯胺能与BSA形成复合物而导致BSA内源性荧光猝灭,猝灭机理为静态猝灭过程。经计算得到了不同酸度和不同温度下对硝基苯胺与BSA反应的结合常数、结合位点数。结合过程的热力学参数变化表明,该相互作用是一个熵增加、Gibbs自由能降低的自发作用过程,其作用力类型主要为静电作用力。The interaction between p-mtroaniline and bovine serum album （BSA） was investigated using fluorescence spectrodcopy at different pH. The experimental results showed that the complex formation between BSA and p-nitroaniline and the fluorescence quenching was a result of the static quenching. The association constants and the number of binding sites were obtained at different pH and different temperature. On the basis of the thermodynamic parameters,the process of binding p-nitroaniline on BSA was a molecular interaction procedure in which entropy increased and Gibbs free energy decreased. The main sort of binding force between p-nitroaniline and BSA is electrostatic force interaction.

关 键 词：对硝基苯胺 牛血清白蛋白 相互作用 

分 类 号：O657.32[理学—分析化学]