摘要
用荧光猝灭法研究了水溶液中辛烷磺酸钠(SOS)与牛血清白蛋白(BSA)的相互结合反应.结果表明,SOS与BSA的相互结合作用为动态猝灭.在水溶液中SOS与蛋白质牢固结合,其结合常数K=4.06×103.根据Frster非辐射能量转移理论,计算了给体与受体间距离r=7.56 nm和能量转移效率E=0.317,并根据热力学参数推测了SOS与BSA的作用力类型及其随BSA浓度的变化.结合红外和溶液中粒径大小的变化初步探讨了BSA构象的变化.
The interactions between sodium 1 octanesulfonate （SOS） and bovine serum albumin （BSA） were studied by fluorescence spectroscopy. The association constant between SOS and BSA was obtained by fluorescence quenching, and the binding constant was 4.06 × 10^3. Based on the Fǒrster theory, the distance between SOS and protein was calculated to he 2. 56 nm . According to the thermodynamic parameters, the main binding force could be judged. The mechanism of quenching belonged to dynamic quenching and the main sort of binding force was hydrophobic force. FT-IR spectra and the change of the particle size were studied on the conformation of BSA.
出处
《湖北大学学报（自然科学版）》
CAS
北大核心
2009年第4期384-387,402,共5页
Journal of Hubei University：Natural Science
基金
"十一五"国家科技支撑计划重点项目(2008BAC32B03)资助
湖北省自然科学基金(2008CDB017)资助
