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机构地区:[1]中国药科大学高职学院,江苏南京211198 [2]南京晓庄学院化学系,江苏南京210017
出 处:《江苏大学学报(医学版)》2009年第5期387-390,共4页Journal of Jiangsu University:Medicine Edition
摘 要:目的:应用光谱技术研究曲克芦丁(troxerutin,TRO)与牛血清白蛋白(bovine serum album in,BSA)间结合作用机制。方法:通过荧光光谱法确定曲克芦丁对BSA的荧光猝灭机制。依据热力学参数讨论两者之间的主要作用力类型。利用同步荧光光谱考察曲克芦丁对BSA构象的影响。结果:曲克芦丁对BSA的荧光猝灭机制为静态猝灭;反应的热力学参数ΔH=-77.06 KJ/mol,ΔS=-152.20 J/(mol.K)。结论:曲克芦丁与BSA之间的主要作用力是范德华力;曲克芦丁的加入使BSA构象发生了变化。Objective: Applied spectroscopy to study the interaction mechanism of troxerutin and bovine serum albumin(BSA).Methods: Fluorescence spectroscopy method was used to determine the fluorescence quenching mechanism of BSA caused by troxerutin.According to the thermodynamic parameters the major force types between troxerutin and BSA was discussd.The effect of troxerutin on bovine serum albumin was also studied by synchronous fluorescence spectrometry.Results: The quenching mechanism of troxerutin to bovine serum albumin was static quenching. The thermodynamic parameters of the reaction was △H =-77.06 KJ/mol,AS = - 152.20 J/( mol·K). Conclusion: The main and BSA was Van derWaals interaction. Troxerutin binding on the bovine serum albumin could change the serum protein conformation.
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