| 光谱法研究牡荆素与蛋白质相互作用及共存金属离子的影响 |
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| 引用本文： | 刘帅涛,陶慧林,寿红娟.光谱法研究牡荆素与蛋白质相互作用及共存金属离子的影响[J].分析试验室,2011,30(8):11-15. |
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| 作者姓名： | 刘帅涛 陶慧林 寿红娟 |
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| 作者单位： | 桂林理工大学化学与生物工程学院,桂林,541004 |
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| 摘 要： | 利用荧光光谱法和紫外-可见光谱法研究了牡荆素(VT)与牛血清白蛋白(BSA)之间的相互作用.VT对BSA的荧光猝灭为动态猝灭过程,测定了不同温度下的猝灭常数；根据F(o)rster非辐射能量转移理论,计算出VT在BSA中的结合位置与色氨酸残基间的距离为2.675.nm；通过热力学参数推断出VT与BSA之间主要靠疏水作用...
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| 关 键 词： | 牡荆素 牛血清蛋白 动态猝灭 金属离子 |
Studies on interaction of vitexin with bovine serum albumin and effect of the coexistent metal ions on the reaction by spectrometry |
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| LIU Shuai-tao,TAO Hui-lin,SHOU Hong-juan.Studies on interaction of vitexin with bovine serum albumin and effect of the coexistent metal ions on the reaction by spectrometry[J].Chinese Journal of Analysis Laboratory,2011,30(8):11-15. |
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| Authors: | LIU Shuai-tao TAO Hui-lin SHOU Hong-juan |
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| Institution: | LIU Shuai-tao,TAO Hui-lin and SHOU Hong-juan(College of Chemical and Bioengineering,Guilin University of technology,Guilin 541004) |
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| Abstract: | The interaction between vitexin and bovine serum albumin(BSA) was studied by fluorescence and UV/Vis absorption spectroscopy.The results revealed that vitexin caused the fluorescence quenching of BSA through a dynamic quenching procedure.The quenching constant was obtained at various temperatures.The binding locality was found to be an area 2.675 nm away from tryptophan residue in BSA based on Frster's non-radiation energy transfer mechanism.The binding power between vitexin and BSA is mainly the hydrophobi... |
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| Keywords: | Vitexin Bovine serum albumin(BSA) Dynamic quenching Coexistent metal ions |
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