荧光光谱法研究锌(Ⅱ)存在下诺氟沙星与牛血清白蛋白的结合作用  

Bovine Serum Albumin in the Presence of Zinc(Ⅱ) by Fluorescence Method

作　　者：吴根华[1] 汪婕[1] 陈金龙[1] 郭畅[1] 王培三[1] 王冬香[1] 汪竹青[1] 

机构地区：[1]安庆师范学院化学化工学院

出　　处：《光谱学与光谱分析》2008年第4期913-916,共4页Spectroscopy and Spectral Analysis

基　　金：国家自然科学基金项目(20371002);安徽省教育厅自然科学基金项目(2002KJ201)资助

摘　　要：在模拟生理条件下,用荧光光谱法研究了诺氟沙星对牛血清白蛋白以及锌(Ⅱ)对诺氟沙星和牛血清白蛋白荧光光谱特性的影响。实验结果表明,诺氟沙星和锌(Ⅱ)都可以使牛血清白蛋白的荧光强度发生猝灭。根据荧光猝灭双倒数图计算诺氟沙星和牛血清白蛋白之间的结合常数为6.80×105,结合位点数为1.21。由此可见,诺氟沙星和牛血清白蛋白之间有很强的结合作用,这为诺氟沙星在体内被蛋白质储存和转运提供了条件。并且在锌(Ⅱ)存在下,诺氟沙星与牛血清白蛋白的结合作用有所增强。荧光猝灭双倒数图计算的结果表明,诺氟沙星和牛血清白蛋白之间的结合常数和结合位点数均随锌(Ⅱ)浓度的增大而增大。通过对锌(Ⅱ)、诺氟沙星和牛血清白蛋白的结合反应的研究,进一步探讨了诺氟沙星、锌(Ⅱ)在生物体内与蛋白质相互作用的机理。The interaction between norfloxacin and bovine serum albumin, and the influence of Zinc（Ⅱ ） on the system of norfloxacin and bovine serum albumin was studied under physiological condition by fluorescence method. It was shown that norfloxacin has a powerful ability to quench the BSA fluorescence via a nonradiative energy transfer mechanism. The fluorescence quenching data were analyzed according to Stern-Volmer equation and double-reciprocal equation, and the binding constant（K） and the binding sites（n） were obtained. In the system of binary complex of NFLX and BSA, K= 6.80×10^5 and n= 1.21. There is a strong combination between NFLX and BSA, which offers the condition for the serum protein to be deposited and transported in vivo. Besides, the combination between NFLX and BSA becomes stronger in the presence of Zinc（Ⅱ）. According to Stern-Volmer equation and double-reciprocal equation, the concentration of Znic（Ⅱ ） is denser, and the binding constant（K） and the binding sites（n） are bigger. By studying the binding interaction between Zinc（Ⅱ）, norfloxacin and BSA, the mechanism of the interaction among norfloxacin, Zinc（ Ⅱ ） and protein in organism, is furtherly discussed.

关 键 词：荧光光谱法 诺氟沙星 锌(Ⅱ) 牛血清白蛋白 结合作用 

分 类 号：R33-33[医药卫生—人体生理学]