| 采用荧光光谱法研究烟酸与牛血清白蛋白的相互作用 |
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| 引用本文： | 蔡向阳,谢勇平,蔡碧琼,郑新宇,李清禄. 采用荧光光谱法研究烟酸与牛血清白蛋白的相互作用[J]. 福建农林大学学报(自然科学版), 2013, 42(1) |
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| 作者姓名： | 蔡向阳 谢勇平 蔡碧琼 郑新宇 李清禄 |
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| 作者单位： | 福建农林大学生命科学学院,福建福州,350002 |
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| 基金项目： | 福建省自然科学基金资助项目 |
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| 摘 要： | 采用荧光光谱法研究了烟酸(NTA)与牛血清白蛋白(BSA)之间的相互作用.结果表明,NTA主要以动态猝灭的方式使BSA的内源性荧光下降.通过计算得出了在测定温度(T)为293和310 K时,NTA与BSA的结合常数(KA)分别为31.9和72.9 L·mol-1.根据热力学参数确定了NTA与BSA之间以疏水力相互作用.同步荧光光谱与紫外光谱技术分析表明,NTA对BSA的构象几乎没有影响.
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| 关 键 词： | 荧光光谱 烟酸 牛血清白蛋白 紫外光谱 |
Studies on infraction between nicotinic acid and bovine serum albumin by fluorescence spectrometry |
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| CAI Xiang-yang , XIE Yong-ping , CAI Bi-qiong , ZHENG Xin-yu , LI Qing-lu. Studies on infraction between nicotinic acid and bovine serum albumin by fluorescence spectrometry[J]. Journal of Fujian Agricultural and Forestry University, 2013, 42(1) |
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| Authors: | CAI Xiang-yang XIE Yong-ping CAI Bi-qiong ZHENG Xin-yu LI Qing-lu |
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| Abstract: | The interaction between nicotinic acid(NTA) and bovine serum albumin(BSA) in physiological solution was investigated by fluorescence spectrometry.The results showed fluorescence intensity of BSA was quenched by NTA based on the dynamic quenching model.The binding constants were obtained by calculation,which were 31.9(293 K) and 72.9 L·mol-1(310 K) respectively.The thermodynamic parameters obtained from measured data showed that the interaction of NTA and BSA was mainly driven by hydrophobic force.Synchronous fluorescence spectrometry and ultraviolet(UV) spectroscopy indicated that NTA did not affect the conformation of BSA. |
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| Keywords: | fluorecense spectrometry nicotinic acid bovine serum albumin ultraviolet spectroscopy |
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