[荧光光谱法研究亚甲蓝与牛血清白蛋白的相互作用]
[Study on the interaction between methylene blue and bovine serum albumin by fluorescence spectroscopy].
作者信息
Yi P G, Liu J F, Shang Z C, Yu Q S
机构信息
Department of Chemical Engineering, Xiangtan Polytechnic University, Xiangtan 411201, China.
出版信息
Guang Pu Xue Yu Guang Pu Fen Xi. 2001 Dec;21(6):826-8.
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 Förester spectroscopy energy transfer. The effect of MB on the conformation of BSA is further analyzed using synchronous fluorescence spectrometry.
采用荧光光谱法研究了水溶液中亚甲蓝（MB）与牛血清白蛋白（BSA）的结合特性。结果表明，平衡常数KA = 3.44×10⁵ L·mol⁻¹，结合位点数n = 1.03，MB对BSA荧光的猝灭机制为静态猝灭过程。基于Förster光谱能量转移理论，得到了MB与BSA之间的结合距离和能量转移效率。利用同步荧光光谱法进一步分析了MB对BSA构象的影响。
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