Zhang H R, Guo S Y, Li L, Cai M Y, Jin W J, Liu C S
Light Industry and Chemical Engineering Research Institute, South China University of Technology, Guangzhou 510640, China.
Guang Pu Xue Yu Guang Pu Fen Xi. 2001 Dec;21(6):829-32.
The binding reaction between sparfloxacion (SPFX) and bovine serum albumin (BSA) or chicken egg albumin (CEA) in aqueous was studied using fluorescence and absorption spectra. Their binding constants are KCEA = 8.29 x 10(6) and KBSA = 4.41 x 10(7), and the binding sites are nCEA = 0.558, nBSA = 0.793 respectively. The action distances (RCEA = 1.99 nm, RBSA = 2.09 nm) and energy transfer efficiencies (ECEA = 0.766, EBSA = 0.714) between donor-acceptor and SPFX were obtained by Förster's nonradiative energy transfer mechanism. The experiment demonstrated that the higher the temperature is, the lower the slopes of quenching curves of BSA and CEA are in presence of different amounts of SPFX. It is confirmed that the combination for SPFX with BSA or CEA is a single static quenching process, their interaction may be interpreted with energy transfer mechanism. Through binding reaction of the two albumins with SPFX, the biological effects and action mechanism of SPFX with albumins in vivo were discussed.
采用荧光光谱和吸收光谱研究了司帕沙星（SPFX）与牛血清白蛋白（BSA）或鸡卵白蛋白（CEA）在水溶液中的结合反应。它们的结合常数分别为KCEA = 8.29×10(6)和KBSA = 4.41×10(7)，结合位点数分别为nCEA = 0.558，nBSA = 0.793。通过Förster非辐射能量转移机制获得了供体 - 受体与SPFX之间的作用距离（RCEA = 1.99 nm，RBSA = 2.09 nm）和能量转移效率（ECEA = 0.766，EBSA = 0.714）。实验表明，温度越高，在不同量SPFX存在下，BSA和CEA猝灭曲线的斜率越低。证实SPFX与BSA或CEA的结合是单一的静态猝灭过程，它们之间的相互作用可用能量转移机制来解释。通过两种白蛋白与SPFX的结合反应，探讨了SPFX与白蛋白在体内的生物学效应及作用机制。
