光谱学与光谱分析 |
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Studies on the Features of Binding Reaction of Eosin Y with Bovine Serum Albumin |
YAN Cheng-nong1,MEI Ping1,XIONG Dan1,LIU Yi2 |
1. College of Chemistry and Environmental Engineering,Yangtze University, Jingzhou 434020, China 2. College of Chemistry and Molecule Sciences, Wuhan University, Wuhan 430072, China |
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Abstract The binding of eosin Y to bovine serum albumin (BSA) was studied by fluorescence spectroscopy and ultraviolet 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,Lineweaver-Burk equation and thermodynamic equation at 298.15 K,the binding constant(KLB=3.601 ×105 L·mol-1) and thermodynamic parameters(ΔHθ:-22.66 kJ·mol-1,ΔGθ:-31.30 kJ·mol-1 and ΔSθ:36.32 J·K-1)were obtained, which provide important information for researching the configuration modification of BSA caused by added eosin Y,biological effects of eosin Y in a living body, and dyeing mechanism of cells.
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Received: 2005-10-26
Accepted: 2006-06-06
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Corresponding Authors:
YAN Cheng-nong
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Cite this article: |
YAN Cheng-nong,MEI Ping,XIONG Dan, et al. Studies on the Features of Binding Reaction of Eosin Y with Bovine Serum Albumin[J]. SPECTROSCOPY AND SPECTRAL ANALYSIS, 2006, 26(12): 2306-2310.
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URL: |
https://www.gpxygpfx.com/EN/Y2006/V26/I12/2306 |
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