摘要
应用荧光光度法研究了水溶液中利福平与牛血清白蛋白分子间的结合反应,讨论了利福平对蛋白质内源荧光的猝灭机理,测定了结合常数(KA=3.1×10-5L·mol-1)和结合位点数(n=1.06)。依据Frster非辐射能量转移理论确定了供体-受体间的结合距离(r=3.89nm)和能量转移效率,并用同步荧光技术考察了利福平对牛血清白蛋白构象的影响。
Intermolecular combination of rifampin with bovine serum albumin （BSA） in aqueous solution was studied by fluorospectrophotometry. Mechanism of quenching of fluorescence of BSA by rifampin was discussed. Equilibrium constant of combination （KA） and number of combination site （n） were determined and values obtained were 3.1×10^-5 L·mol^-1 and 1. 06 respectively. By the Forster non-radiating energy transfer theory, the combination distance between the donor and acceptor as well as the efficiency of energy transfer were determined, and the value of combination distance （r） was found to be 3. 89 nm. Effect of rifampin on the configuration of BSA was studied by the synchronous fluorospectrophotometry.
出处
《理化检验（化学分册）》
CAS
CSCD
北大核心
2008年第3期261-263,共3页
Physical Testing and Chemical Analysis(Part B:Chemical Analysis)
基金
聊城大学科研基金(X061003)
关键词
荧光光度法
结合反应
利福平
牛血清白蛋白
Fluorospectrophotometry
Combination reaction
Rifampin
Bovine serum albumin
