Fluorescence Studies on the Interactions of Barbaloin with Bovine Serum Albumin
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概要
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The fluorescence quenching reactions of barbaloin with bovine serum albumin (BSA) in pH 7.20 Tris-HCl buffer solution were studied. The quenching mechanism of BSA by barbaloin was interpreted using the Stern-Volmer (S-V) mechanism. The binding constant K values were 2.78×10^5 (293 K), 1.87×10^5 (310 K), 1.25×10^5 (318K), and the number of binding sites (n) were 1.18, 1.14, and 1.09, respectively. In addition, the thermodynamic functions enthalpy (ΔH°) and entropy (ΔS°) for the reaction were also calculated according to Vant's Hoff equation were -23.7 kJ/mol and 23.6 J/mol, respectively. Plausible explanations of the quenching mechanism are discussed on the basis of a hydrophobic interaction between barbaloin and BSA.
- 公益社団法人日本薬学会の論文
- 2003-05-01
著者
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Tian Jianniao
Department Of Chemistry Lanzhou University
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Hu Zhide
Department Of Chemistry Lanzhou University
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LIU Jiaqin
Department of Chemistry, Lanzhou University
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ZHANG Jiyou
Department of Chemistry, Lanzhou University
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CHEN Xinguo
Department of Chemistry, Lanzhou University
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Zhang Jiyou
Department Of Chemistry Lanzhou University
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Liu Jiaqin
Department Of Chemistry Lanzhou University
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Chen Xinguo
Department Of Chemistry Lanzhou University
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