磺基水杨酸与牛血清白蛋白相互作用的荧光法研究  

Fluorescence Study on the Interaction Between 5-sulfosalicylic Acid and Bovine Serum Albumin

作　　者：李娜[1] 张玉平[1] 魏永巨[1] 

机构地区：[1]河北师范大学化学学院,河北石家庄050016

出　　处：《河北师范大学学报（自然科学版）》2004年第1期50-54,共5页Journal of Hebei Normal University：Natural Science

基　　金：河北省自然科学基金资助项目(200153);河北省教育厅博士基金资助项目

摘　　要：用荧光法研究了5磺基水杨酸(SSA)与牛血清白蛋白(BSA)之间的相互作用.实验发现SSA可以猝灭BSA的荧光,同时自身的荧光敏化增强,表明两者之间发生了能量转移.能量转移的机理是BSA与SSA结合形成了复合物.SSA在BSA212位色氨酸残基附近的结合数为1,结合常数为6.5×105.疏水力是结合反应的主要作用力.基于Forster能量转移理论确定了SSA与BSA212位色氨酸残基间的距离为1.55nm.研究了实验条件对反应的影响,在pH4.0～8.0之间,BSASSA复合物基本稳定,离子强度对复合物形成有明显影响.Interaction between 5-sulfosalicylic acid (SSA) and bovine serum albumin (BSA) was studied by fluorescence method.It was found that fluorescence of BSA were quenched by SSA,meanwhile the fluorescence of SSA enhanced,indicating that an energy transfer between BSA and SSA had been occurred.The mechanism of energy transfer was considered to be the formation of BSA-SSA complex.The binding number of SSA on the vicinity of 212-tryptophane residue of BSA was determined to be 1,and the binding constant was 6.5×10~5.Hydrophobic force is the main binding force between SSA and BSA.Based on Forster energy transfer theory,the distance between 212-tryptophane residue of BSA and SSA was determined to be 1.55*!nm.Effects of experimental conditions on the interaction were investigated.At pH 4.0～8.0,BSA-SSA complex were essentially stable,ionic strength had a significant influence on the formation of complex.

关 键 词：磺基水杨酸 牛血清白蛋白 荧光法 Forster能量转移理论 生物医学研究 

分 类 号：Q51[生物学—生物化学] R318[医药卫生—生物医学工程]