光谱学与光谱分析 |
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Bovine Serum Albumin in the Presence of Zinc(Ⅱ) by Fluorescence Method |
WU Gen-hua1,2,WANG Jie1,2,CHEN Jin-long1,GUO Chang1,WANG Pei-san1,2,WANG Dong-xiang1,2,WANG Zhu-qing1,2 |
1. College of Chemistry and Chemical Industry, Anqing Teachers College, Anqing 246003, China 2. College of Chemistry and Materials Science, Anhui Normal University, Wuhu 241000, China |
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Abstract 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=6.80×105 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.
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Received: 2006-12-02
Accepted: 2007-03-06
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Corresponding Authors:
WU Gen-hua
E-mail: wugenh@aqtc.edu.cn
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