[Studies on the reaction of balofloxacin with bovine serum albumin].
Zheng-Yu Yan, Xiu-Fen Shao, Xin-Min Jiang, Yu-Zhu Hu
Index: Guang Pu Xue Yu Guang Pu Fen Xi 26(8) , 1494-8, (2006)
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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 Forster 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.
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