通过紫外吸收光谱法、紫外二阶导数光谱法和荧光光谱法研究了生理pH值条件、紫外照射(UV C 253.7nm)下Pb(Ⅱ)与牛血清白蛋白(BSA)的相互作用。紫外光谱和紫外二阶导数光谱显示紫外光照射改变了蛋白质中氨基酸残基的微环境。Stern-Volme...通过紫外吸收光谱法、紫外二阶导数光谱法和荧光光谱法研究了生理pH值条件、紫外照射(UV C 253.7nm)下Pb(Ⅱ)与牛血清白蛋白(BSA)的相互作用。紫外光谱和紫外二阶导数光谱显示紫外光照射改变了蛋白质中氨基酸残基的微环境。Stern-Volmer方程和Lineweaver-Burk方程分析表明,经紫外光照射后,Pb(Ⅱ)对BSA的荧光猝灭作用依然为静态猝灭作用,且没有改变其强结合位点的位置。受紫外照射过的BSA加入Pb(Ⅱ)后,BSA与Pb(Ⅱ)的结合常数(KS)随着照射时间的延长而逐渐降低;而BSA与Pb(Ⅱ)先混合后照射时,结合常数(KS)随着照射时间的延长却逐渐升高。展开更多
The interaction of Co（Ⅱ） with BSA under UV C （253.7 nm） irradiation under physiological conditions has been studied by UV-vis spectrum, ultraviolet second-derivative spectroscopy and fluorescence spectrum. The qu...The interaction of Co（Ⅱ） with BSA under UV C （253.7 nm） irradiation under physiological conditions has been studied by UV-vis spectrum, ultraviolet second-derivative spectroscopy and fluorescence spectrum. The quenching rate constant kq and the association constant Ka were calculated according to Stern-Volmer equation based on the quenching of the fluorescence of BSA by Co（Ⅱ）.展开更多
文摘通过紫外吸收光谱法、紫外二阶导数光谱法和荧光光谱法研究了生理pH值条件、紫外照射(UV C 253.7nm)下Pb(Ⅱ)与牛血清白蛋白(BSA)的相互作用。紫外光谱和紫外二阶导数光谱显示紫外光照射改变了蛋白质中氨基酸残基的微环境。Stern-Volmer方程和Lineweaver-Burk方程分析表明,经紫外光照射后,Pb(Ⅱ)对BSA的荧光猝灭作用依然为静态猝灭作用,且没有改变其强结合位点的位置。受紫外照射过的BSA加入Pb(Ⅱ)后,BSA与Pb(Ⅱ)的结合常数(KS)随着照射时间的延长而逐渐降低;而BSA与Pb(Ⅱ)先混合后照射时,结合常数(KS)随着照射时间的延长却逐渐升高。
基金Project supported by the National Natural Science Foundation of China （No. 20671023）, the Science Foundation of Guangxi Province, China, and the Teaching and Research Award Programme for 0utstanding Young Teachers in Higher Education Institutions of Ministry of Education, China.
文摘The interaction of Co（Ⅱ） with BSA under UV C （253.7 nm） irradiation under physiological conditions has been studied by UV-vis spectrum, ultraviolet second-derivative spectroscopy and fluorescence spectrum. The quenching rate constant kq and the association constant Ka were calculated according to Stern-Volmer equation based on the quenching of the fluorescence of BSA by Co（Ⅱ）.
