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荧光光谱法研究辛烷磺酸钠与BSA的相互作用
引用本文:李玲,徐祖顺,宋功武.荧光光谱法研究辛烷磺酸钠与BSA的相互作用[J].湖北大学学报(自然科学版),2009,31(4):384-387.
作者姓名:李玲  徐祖顺  宋功武
作者单位:湖北大学化学与化工学院;湖北大学材料科学与工程学院;
基金项目:“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
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=4.06×10^3.根据Fǒrster非辐射能量转移理论,计算了给体与受体间距离r=7.56nm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.

关 键 词:辛烷磺酸钠  牛血清白蛋白  荧光猝灭  结合反应

Study on the interaction between sodium octanesulfonate and bovine serum albumin by spectroscopic analysis
LI Ling,XU Zu-shun,SONG Gong-wu.Study on the interaction between sodium octanesulfonate and bovine serum albumin by spectroscopic analysis[J].Journal of Hubei University(Natural Science Edition),2009,31(4):384-387.
Authors:LI Ling  XU Zu-shun  SONG Gong-wu
Institution:1.School of Chemistry and Chemical Engineering;Hubei University;Wuhan 430062 China;2.School of Materials Science and Engineering;Wuhan 430062 China
Abstract: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.
Keywords:surfactant  BSA  quenching  energy transfer  interaction  
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