| 核黄素与牛血清白蛋白相互作用的荧光光谱研究 |
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| 引用本文： | 尚永辉,李华,孙家娟,郑敏燕. 核黄素与牛血清白蛋白相互作用的荧光光谱研究[J]. 分析科学学报, 2010, 26(1). DOI: 10.3969/j.issn.1006-6144.2010.01.016 |
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| 作者姓名： | 尚永辉 李华 孙家娟 郑敏燕 |
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| 作者单位： | 咸阳师范学院化学与化工学院,陕西咸阳,712000;西北大学分析科学研究所,陕西西安,710069;西北大学分析科学研究所,陕西西安,710069;咸阳师范学院化学与化工学院,陕西咸阳,712000 |
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| 基金项目： | 西北大学研究生交叉学科资助项目(07YJC09);;陕西省教育厅基金(06JK164,07JK426);;咸阳师范学院专项科研基金(08XSYK218,05XSYK105) |
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| 摘 要： | 采用荧光猝灭光谱、同步荧光光谱研究了核黄素与牛血清白蛋白(BSA)相互作用的光谱行为。结果发现,在温度为293 K和310 K时核黄素与BSA的结合常数(Kb)分别为4.879×105L.mol-1和1.880×105L.mol-1,结合热力学方程计算得到了对应温度下的热力学参数。结果表明核黄素对BSA有较强的荧光猝灭作用,其荧光猝灭过程属于动态猝灭机制,二者主要靠疏水作用力结合。采用同步荧光光谱探讨了核黄素对BSA构象的影响。
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| 关 键 词： | 核黄素 牛血清白蛋白 荧光光谱 |
Study on the Interaction of Bovine Serum Albumin with Riboflavin by Fluorescence Spectroscopy |
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| SHANG Yong-hui,LI Hua,SUN Jia-juan,ZHENG Min-yan. Study on the Interaction of Bovine Serum Albumin with Riboflavin by Fluorescence Spectroscopy[J]. Journal of Analytical Science, 2010, 26(1). DOI: 10.3969/j.issn.1006-6144.2010.01.016 |
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| Authors: | SHANG Yong-hui LI Hua SUN Jia-juan ZHENG Min-yan |
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| Affiliation: | 1.School of Chemistry & Chemical Engineering;Xianyang Normal University;Xianyang712000;2.Institute of Analytical Science;Northwest University;Xi'an 710069 |
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| Abstract: | The binding reaction of riboflavin with bovine serum albumin was studied by fluorescence spectroscopy. It was shown that riboflavin had a strong ability of quenching the fluorescence of BSA. The Stem-Volmer curve and double logarithm equation of the fluorescence quenching of BSA by riboflavin indicated that the quenching mechanism was a dynamic quenching; the binding constants(K_(SV)) were 1.3658×10~5 L·mol~(-1)(293 K) and 1.5082×10~5 L·mol~(-1)(310 K), respectively. The thermodynamic parameters showed that the interaction of riboflavin and BSA was mainly driven by hydrophobic force. Synchronous spectroscopy was used to investigate the conformational changes of BSA. |
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| Keywords: | Riboflavin Bovine serum albumin(BSA) Fluorescence spectroscopy |
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