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  • Title: [Studies on the features of binding reaction of eosin Y with bovine serum albumin].
    Author: Yan CN, Mei P, Xiong D, Liu Y.
    Journal: Guang Pu Xue Yu Guang Pu Fen Xi; 2006 Dec; 26(12):2306-10. PubMed ID: 17361737.
    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 x 10(5) L x mol(-1)) and thermodynamic parameters (deltaHtheta: - 22. 66 kJ x mol(-1), deltaGtheta: -31. 30 kJ x mol(-1) and deltaStheta: 36.32 J x 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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