牛血清白蛋白与铬(VI)相互作用的荧光光谱法研究  

Studies on the Interaction for Bovine Serum Albumin with Cr(VI)by Fluorescence Spectra

作　　者：高旭[1] 李树伟[1] 马玉洁[1] 张贝克[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

出　　处：《西部皮革》2011年第22期30-33,共4页West Leather

基　　金：重庆市教委(批准号:KJ051201)项目资助

摘　　要：基于模拟动物体生理条件下,采用荧光猝灭光谱法研究了牛血清白蛋白(BSA)与铬(VI)的相互作用,试验发现C(rVI)对BSA有较强的荧光猝灭作用。通过Stern-Volmer方程,Lineweaver-BurK方程和双倒数曲线处理实验数据,表明C(rVI)与BSA属于静态荧光猝灭,测定了C(rVI)对BSA的猝灭常数,确定了C(rVI)与BSA结合位点数均为2。并根据热力学参数计算了C(rVI)与BSA之间的作用力类型主要为疏水作用。并用同步荧光技术研究了C(rVI)对BSA构象的影响。Under the imitated physiological condition of animal body, The binding Cr （VI）was studied by fluorescence spectroscopy. The quenching mechanism of in reaction of BSA with trinsic fluorescence of BSA with Cr（VI）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 between BSA and Cr （VI）were measured, and all of the numbers of binding sites are 2.The thermodynamic parameter of binding reaction was determined by the binding, it＇s showed the interaction between BSA and Cr （VI）were driven mainly by hydrophobic force . Synchronous spectroscopy was used to investigate the conformational changes of BSA.

关 键 词：牛血清白蛋白 铬(VI) 荧光光谱 相互作用 

分 类 号：TS57[轻工技术与工程—皮革化学与工程]