Abstract：In the present paper, a fluorescence method was used to study at different pH the fluorescence quenching of bovine serum albumin (BSA) by its interaction with balofloxacin (BLFX). The interaction association constants of BSA and BLFX were determined from a double reciprocal line Weaver-Burk plot. According to the Frster dipole-dipole energy transfer, the distance to be measured between the BLFX and tryptophane is 5.09 nm. From thermodynamical coordination it can be judged that the binding power between BLFX and BSA is electrostatic effect. The effect of BLFX on the conformation of BSA was also analyzed by using synchronous fluorescence spectroscopy.
严拯宇，邵秀芬，姜新民，胡育筑. 巴洛沙星与牛血清白蛋白相互作用的研究[J]. 光谱学与光谱分析, 2006, 26(08): 1494-1498.
YAN Zheng-yu, SHAO Xiu-fen, JIANG Xin-min, HU Yu-zhu. Studies on the Reaction of Balofloxacin with Bovine Serum Albumin. SPECTROSCOPY AND SPECTRAL ANALYSIS, 2006, 26(08): 1494-1498.
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