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荧光光谱法研究黄豆黄素与牛血清白蛋白的相互作用
引用本文:宋胜梅,李艺敏,徐茂田,屈凌波. 荧光光谱法研究黄豆黄素与牛血清白蛋白的相互作用[J]. 光谱实验室, 2011, 28(2): 618-622
作者姓名:宋胜梅  李艺敏  徐茂田  屈凌波
作者单位:1. 商丘师范学院化学系河南省高校重点实验室培育基地,河南省商丘市文化路298号,476000;郑州大学化学系,郑州市,450001
2. 商丘师范学院化学系河南省高校重点实验室培育基地,河南省商丘市文化路298号,476000
3. 郑州大学化学系,郑州市,450001
摘    要:用荧光光谱法在pH 7.4的PBS中研究了黄豆黄素(Glycitein,GL)与牛血清白蛋白(Bovine serum albumin,BSA)分子之间的相互作用方式及机理.结果表明GL可静态猝灭BSA的内源荧光.310K和315K的结合位点数与表观结合常数分别为1.30,8.09×104L·mol-1和1.73,5....

关 键 词:黄豆黄素  牛血清白蛋白  荧光光谱  相互作用

Study on the Interaction Between Glycitein and BSA by Fluorescence Spectroscopy
SONG Sheng-Mei,LI Yi-Min,XU Mao-Tian,QU Ling-Bo. Study on the Interaction Between Glycitein and BSA by Fluorescence Spectroscopy[J]. Chinese Journal of Spectroscopy Laboratory, 2011, 28(2): 618-622
Authors:SONG Sheng-Mei  LI Yi-Min  XU Mao-Tian  QU Ling-Bo
Affiliation:SONG Sheng-Meia,b LI Yi-Mina XU Mao-Tiana QU Ling-Boba(Henan Key Laboratory Cultivation Base of Nanobiological Analytical Chemistry,Department of Chemistry,Shangqiu Normal University,Shangqiu,Henan 476000,P.R.China)b(Department of Chemistry,Zhengzhou University,Zhengzhou 450001,P.R.China)
Abstract:The interaction mechanism and mode of glycitein(GL)with bovine serum albumin(BSA) in pH 7.4 PBS was studied by fluorescence spectroscopy.The intrinsic fluorescence of BSA could be quenched by GL.Further more,the numbers of binding site were 1.30 and 1.73 while the apparent binding constants were 8.09×104L·mol-1 and 5.22×104L·mol-1 at 310K and 315K,respectively.The thermodynamic parameters had indicated that the type of force was hydrogen bonding and Van-der Waals force.Synchronous fluorescence spectra showed that the structure of BSA was changed when GL was added.The method could be significant for understanding the interaction mechanism between GL and proteins.
Keywords:Glycitein  Bovine Serum Albumin  Fluorescence Spectra  Interaction  
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