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甘草酸单铵盐牛血清白蛋白超分子体系的荧光光谱研究

Fluorescence Spectroscopic Study on the Monoammonium Glycyrrhizinate-Bovine Serum Albumin Supramolecular System

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【作者】 俞英; 周震涛;

【Author】 YU Ying~ 1, 2, ZHOU Zhen-tao~1 1. College of Material Science and Engineering, South China University of Technology, Guangzhou 510640, China 2. Department of Chemistry, South China Normal University, Guangzhou 510631, China

【机构】 华南理工大学材料科学与工程学院; 华南理工大学材料科学与工程学院 广东广州510640华南师范大学化学系; 广东广州510631; 广东广州510640;

【摘要】 对甘草酸单铵盐(MAG)牛血清白蛋白(BSA)体系的荧光光谱进行了研究,采用同步荧光技术考察了甘草酸单铵盐对牛血清白蛋白构象的影响,认为甘草酸单铵盐(MAG)对牛血清白蛋白(BSA)体系荧光猝灭是由于生成了超分子复合物的静态猝灭,求得MAGBSA的形成常数KA及热力学函数ΔG,ΔH和ΔS,根据热力学函数确定了超分子间的作用力类型为静电作用力,依据Forster非辐射能量转移机制,确定了给体受体间的结合距离和能量转移效率。

【Abstract】 The fluorescence quenching mechanism of bovine serum albumin (BSA) by monoammonium glycyrrhizinate (MAG) has been studied. It is proved that static quenching exists in the MAG-BSA supramolecular complex. The formation constant K_A and the thermodynamic functions (such as ΔG, ΔH and ΔS) for the reaction have been all obtained. According to the thermodynamic parameters, the main sort of binding force was electrostatic force. The effect of various metal ions and temperatures on the formation constant of MAG with BSA was also studied. The binding distance between MAG and BSA and the transfer efficiency have been obtained based on the mechanism of Frster energy transfer. The effect of MAG on the conformation of BSA has also been analyzed using synchronous fluorescence spectroscopy.

【基金】 广东省教育厅“千百十工程”优秀人才培养基金(QX02030)资助项目
  • 【文献出处】 光谱学与光谱分析 ,Spectroscopy and Spectral Analysis , 编辑部邮箱 ,2005年09期
  • 【分类号】R96;
  • 【被引频次】11
  • 【下载频次】285
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