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出 处:《激光生物学报》2011年第5期607-612,共6页Acta Laser Biology Sinica
基 金:The Korean government(MEST) Grant(NO 2009-0072927)
摘 要:用荧光光谱法研究诺氟沙星与牛血清白蛋白之间的结合作用,确定了诺氯沙星与牛血清白蛋白的荧光猝灭机制为静态猝灭。通过测定和计算不同温度下该结合反应的结合常数和结合位点数,并根据热力学方程求得了结合反应的热力学参数,讨论了两者间的主要作用力类型是范德华力和氢键。同时采用同步荧光技术考察了诺氟沙星对BSA构象的影响。并从荧光寿命进一步证明诺氟沙星与牛血清白蛋白的荧光猝灭机制为静态猝灭。The quenching mechanism of the fluorescence of BSA with Norfloxacin was studied by fluorescence method. The results showed that the quenching mechanism of Norfloxacin to BSA was static quenching. The binding constants, the number of binding sites and the thermodynamic parameters of the reaction of Norfloxaein with BSA were determined at different temperatures. Therefore the binding forces was mainly H-bond and Van der Waals. The effect of Norfloxacin on the conformation of BSA was also studied by using synchronous fluorescence spectroscopy.
关 键 词:诺氟沙星 牛血清白蛋白(BSA) 荧光光谱 热力学参数 荧光寿命
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