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 。
The binding characteristics of methylene blue (NIB) and bovine serum albumin (BSA) has been studied by fluorescence spectroscopy in aqueous solution. The results show that the equilibrium constant K-A = 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 NIB is a static quenching procedure. The binding distance between MB and BSA and the energy transfer efficiency are obtained based on the theory of Forester spectroscopy energy transfer. The effect of MB on the conformation of BSA is further analyzed using synchronous fluorescence spectrometry.
出处
《光谱学与光谱分析》
SCIE
EI
CAS
CSCD
北大核心
2001年第6期826-828,共3页
Spectroscopy and Spectral Analysis
基金
国家自然科学基金资助项目 (批准号 :2 96330 2 0 )
