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通过荧光猝灭光谱研究了15℃和37℃下水溶液中加替沙星(HGA)与牛血清白蛋白(BSA)的结合作用。由Stern-Volmer曲线计算出双分子猝灭速率常数分别为:Kq=9.28×1012L·mol-1·s-1(15℃),Kq=8.51×1012L·mol-1·s-1 (37 ℃)。结果显示,HGA对BSA的荧光猝灭机理是一种静态猝灭过程。本文获得的热力学参数表明HGA主要以静电引力与BSA结合。HGA的浓度与BSA的荧光强度之间关系的研究表明,HGA与BSA按1 :1摩尔比结合,结合反应的平衡常数K0= 6.80×104 L·mol-1。另外,通过Förster原理计算了HGA与BSA的结合距离及能量转移效率。 相似文献
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Studies on Interaction between Gatifloxacin and Bovine Serum Albumin by Spectroscopy 总被引:1,自引:0,他引:1
The interaction of gatifloxacin (HGA) with bovine serum albumin (BSA) at 15 and 37 ℃ has been investigated by fluorescence quenching spectroscopy in aqueous solution. The bimolecular quenching rate constant was determined by Stem-Volmer curves and the values were Kq=9.28× 10^12 L·mol^-1·s^-1 (15 ℃) and Kq=8.51 ×10^12 L·mol^-1·s^-1 (37 ~C). The results showed that the fluorescence quenching mechanism of BSA by HGA was a static quenching procedure. The thermodynamic parameters indicated that electrostatic forces played major role in the interaction of BSA with HGA. Studies on the relationship between the concentration of HGA and the fluorescence intensity of BSA showed that BSA and HGA bound at the molar ratio 1 : 1 and the equilibrium constant K0 was 6.80 ×10^4 L·mol^-1. The binding distances between BSA and HGA and the energy transfer efficiency were obtained based on the Ftrster's theory. 相似文献
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