| 光谱学与光谱分析 |
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| Study on the Binding Reaction Features Between Naphthol Green B and Bovine Serum Albumin by Fluorescence Spectrophotometry |
| YAN Cheng-nong1,XIE Ze-yu1,MEI Ping1,LIU Yi2 |
1. College of Chemistry and Enviornmental Engineering, Yangtze University, Jinzhou 434023, China
2. College of Chemistry and Molecule Sciences, Wuhan University, Wuhan 430072，China |
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Abstract At different temperatures, the binding of naphthol green B(NGB) to bovine serum albumin (BSA) was studied by the fluorescence spectroscopy, three-dimensional fluorescence spectrum, synchronous fluorescence spectrum and ultra-violet spectrum. It was shown that this compound has a quite strong ability to quench the fluorescence from BSA. After analyzing the fluorescence quenching data according to Sterm-Volmer equation and Lineweaver-Burk equation, it was found that BSA had reacted with naphthol green B and formed a new compound, the quenching action was due to static fluorescence quenching, and the action force was electrostatic interaction. According to the Lineweaver-Burk equation and thermodynamic equation, the average value of the binding constant(KLB：1.411×105 L·mol-1)，the thermodynamic parameters(ΔHθ：-5.707 kJ·mol-1,ΔGθ：-30.25 kJ·mol-1 and ΔSθ：79.95 J·K-1) and the amounts of binding sites(1.258) were obtained, providing important information for the research on the configuration modification of BSA because of the added naphthol green B, biological effects in a living body, and the coloration mechanism of naphthol green B.
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Received: 2006-08-02
Accepted: 2007-01-28
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Corresponding Authors:
YAN Cheng-nong
E-mail: yancn0405@163.com
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| Cite this article: |
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YAN Cheng-nong,XIE Ze-yu,MEI Ping, et al. Study on the Binding Reaction Features Between Naphthol Green B and Bovine Serum Albumin by Fluorescence Spectrophotometry [J]. SPECTROSCOPY AND SPECTRAL ANALYSIS, 2007, 27(12): 2542-2545.
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| URL: |
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https://www.gpxygpfx.com/EN/Y2007/V27/I12/2542 |
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