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
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.
颜承农1, 梅平1,熊丹1,刘义2 . 曙红Y与牛血清白蛋白结合反应特征研究[J]. 光谱学与光谱分析, 2006, 26(12): 2306-2310.
YAN Cheng-nong1,MEI Ping1,XIONG Dan1,LIU Yi2 . Studies on the Features of Binding Reaction of Eosin Y with Bovine Serum Albumin. SPECTROSCOPY AND SPECTRAL ANALYSIS, 2006, 26(12): 2306-2310.
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