牛血清白蛋白与镧(Ⅲ)相互作用的荧光光谱法研究  

Studies on the Interaction for Bovine Serum Albumin with La(Ⅲ)by Fluorescence Spectra

作　　者：高旭[1] 余江[2] 马玉洁[1] 张贝克[1] 李树伟[1] 

机构地区：[1]四川师范大学化学与材料科学学院,四川成都610068 [2]四川大学建筑与环境学院,四川成都610065

出　　处：《稀土》2012年第5期7-10,共4页Chinese Rare Earths

基　　金：国家自然科学基金项目资助(31100374);四川省科技计划项目资助(2011JY0026)

摘　　要：基于模拟生理条件下,采用荧光猝灭光谱法研究了牛血清白蛋白(BSA)与镧(La(Ⅲ))的相互作用,并用同步荧光技术研究了La(Ⅲ)对BSA构象的影响。通过Stern-Volmer方程,Lineweaver-Burk方程和双倒数曲线方程处理实验数据,表明BSA与La(Ⅲ)属于静态荧光猝灭,测定了La(Ⅲ)对BSA的猝灭常数和扩散常数,确定了La(Ⅲ)与BSA结合位点数均为2.673。根据热力学参数计算得知La(Ⅲ)主要通过氢键作用力、范德华尔斯作用力进入BSA亚结构形成的空腔中。Under the imitated physiological condition of animal body,the binding reaction of BSA with La（Ⅲ） was studied by fluorescence spectroscopy and synchronous spectroscopy was used to investigate the conformational changes of BSA.The quenching mechanism of intrinsic fluorescence of BSA with La（Ⅲ） was studied by Stern-volmer curve,Lineweaver-Burk curve and double reciprocal curve.The experimental results showed that static quenching were the main factors of the quenching mechanism of intrinsic fluorescence.The quenching constants and diffusion constants between BSA and La（Ⅲ） were measured,and all of the numbers of binding sites are 2.673.The thermodynamic parameter of binding reaction was determined by the binding,it＇s showed La（Ⅲ） into the cavity formed in the sub-structure of BSA mainly by Hydrogen bonding、Vander force Walls.

关 键 词：牛血清白蛋白 镧 荧光光谱 相互作用 

分 类 号：O657.3[理学—分析化学]