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荧光光谱法研究亚甲基蓝与蛋白质的结合反应
引用本文:易平贵,刘俊峰,商志才,俞庆森.荧光光谱法研究亚甲基蓝与蛋白质的结合反应[J].光谱学与光谱分析,2001,21(6):826-828.
作者姓名:易平贵  刘俊峰  商志才  俞庆森
作者单位:1. 湘潭工学院化工系,湖南,湘潭,411201
2. 浙江大学化学系,浙江,杭州,310027
基金项目:国家自然科学基金资助项目 (批准号 :2 96330 2 0 )
摘    要:应用荧光光谱法研究了水溶液中亚甲基蓝与牛血清白蛋白分子间的结合反应 ,讨论了亚甲基蓝对蛋白质内源荧光的猝灭机理 ,测定了结合常数 (KA=3 44× 10 5L·mol-1)和结合位点数 (n =1 0 3)。依据F rster非辐射能量转移 ,理论确定了授体 受体间的结合距离 (r=1 6 7nm)和能量转移效率 ,并用同步荧光技术考察了亚甲基蓝对牛血清白蛋白构象的影响

关 键 词:荧光光谱  亚甲基蓝  牛血清白蛋白  结合反应  荧光猝灭  相互作用
文章编号:1000-0593(2001)06-0826-03
修稿时间:2000年6月30日

Study on the Interaction between Methylene Blue and Bovine Serum Albumin by Fluorescence Spectroscopy
YI Ping gui ,LIU Jun feng ,SHANG Zhi cai ,and YU Qing sen.Study on the Interaction between Methylene Blue and Bovine Serum Albumin by Fluorescence Spectroscopy[J].Spectroscopy and Spectral Analysis,2001,21(6):826-828.
Authors:YI Ping gui  LIU Jun feng  SHANG Zhi cai  and YU Qing sen
Institution:Department of Chemical Engineering, Xiangtan Polytechnic University, Xiangtan 411201, China.
Abstract:The binding characteristics of methylene blue (MB) and bovine serum albumin (BSA) has been studied by fluorescence spectroscopy in aqueous solution. The results show that the equilibrium constant KA = 3.44 x 10(5) L.mol-1, the number of binding sites n = 1.03, and the quenching mechanism of fluorescence of BSA by MB is a static quenching procedure. The binding distance between MB and BSA and the energy transfer efficiency are obtained based on the theory of F?rester spectroscopy energy transfer. The effect of MB on the conformation of BSA is further analyzed using synchronous fluorescence spectrometry.
Keywords:Fluorescence spectroscopy  Methylene blue  Bovine serum albumin
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