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硒酸钠与牛血清白蛋白相互作用的机理分析
作者姓名:韩晓乐  李擎宇  郝浩  刘晨音  雷佳文  于帆  胡军成
作者单位:中南民族大学化学与材料科学学院
基金项目:国家自然科学基金资助项目(21503283);中央高校基本科研业务费专项资金资助项目(CZQ13003,YCZW15109);湖北省青年基金资助项目(2015CFC875).
摘    要:在模拟动物体生理条件下,采用荧光光谱、紫外-可见吸收光谱等方法研究不同温度下硒酸钠与牛血清白蛋白的相互作用,并通过计算二者相互作用时的热力学参数及检测硒酸钠对牛血清白蛋白构象的影响,对其相互作用机理进行分析。结果表明,硒酸钠对牛血清白蛋白的荧光有猝灭效应,二者反应形成复合物,硒酸钠对牛血清白蛋白的荧光猝灭方式属于静态猝灭;硒酸钠与牛血清白蛋白主要靠静电相互作用力结合,且相互作用是自发进行的,二者的结合位点约为1。

关 键 词:硒酸钠  牛血清白蛋白  相互作用  光谱法  热力学  荧光猝灭
收稿时间:2018/12/10 0:00:00

Mechanism of interaction between sodium selenate and bovine serum albumin
Authors:Han Xiaole  Li Qingyu  Hao Hao  Liu Chenyin  Lei Jiawen  Yu Fan and Hu Juncheng
Institution:College of Chemistry and Material Sciences, South-Central University for Nationalities, Wuhan 430074, China,College of Chemistry and Material Sciences, South-Central University for Nationalities, Wuhan 430074, China,College of Chemistry and Material Sciences, South-Central University for Nationalities, Wuhan 430074, China,College of Chemistry and Material Sciences, South-Central University for Nationalities, Wuhan 430074, China,College of Chemistry and Material Sciences, South-Central University for Nationalities, Wuhan 430074, China,College of Chemistry and Material Sciences, South-Central University for Nationalities, Wuhan 430074, China and College of Chemistry and Material Sciences, South-Central University for Nationalities, Wuhan 430074, China
Abstract:Under simulated animal physiological conditions, the interaction between sodium selenate and bovine serum albumin at different temperatures was studied by fluorescence spectra, uv-vis absorption spectra and other methods. The mechanism of the interaction was analyzed by calculating the thermodynamic parameters of the interaction and measuring the effect of sodium selenate on the conformation of bovine serum albumin. The results show that sodium selenate has quenching effect on the fluorescence of bovine serum albumin. Those two react with each other and form a compound. The quenching behavior of sodium selenate in bovine serum albumin fluorescence quenching process is static quenching. The binding process between sodium selenate and bovine serum albumin is mainly driven by electrostatic force and the interaction is spontaneous, with binding site approximately at 1.
Keywords:sodium selenate  bovine serum albumin  interaction  spectrometry  thermodynamics  fluorescence quenching
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