首页 | 本学科首页   官方微博 | 高级检索  
检索        

荧光猝灭法对葫芦巴碱与人血清白蛋白间相互作用的研究
引用本文:吴文华,赵妍,曹燚,韩凤梅,陈勇.荧光猝灭法对葫芦巴碱与人血清白蛋白间相互作用的研究[J].中医药学报,2010,38(6):57-59.
作者姓名:吴文华  赵妍  曹燚  韩凤梅  陈勇
作者单位:湖北大学中药生物技术省重点实验室,湖北武汉430062
基金项目:湖北省杰出青年基金,中药生物技术省重点实验室开放基金
摘    要:目的:研究葫芦巴碱与人血清白蛋白间的相互作用。方法:在pH 7.4作用液、286nm激发波长条件下采用荧光光谱法来研究不同浓度的葫芦巴碱对人血清白蛋白的荧光猝灭作用。结果:当作用温度为37℃和47℃时,葫芦巴碱与人血清蛋白间的结合常数K分别为749.03L.mol-1和106.29L.mol-1,结合位点数n分别为1.0077和0.7625。结论:葫芦巴碱对人血清白蛋白的荧光发射有一定的猝灭作用,并且温度的升高不利于两者的结合;同时还证明葫芦巴碱与人血清白蛋白分子间的结合力主要是静电作用。

关 键 词:葫芦巴碱  人血清白蛋白  荧光猝灭

Studying on Interaction between Trigonelline and Humen Serum Albumin by Fluorescence Quenching Method
WU Wen-hua,Zhao Yan,Cao Yi,HAN Feng-mei,CHEN Yong.Studying on Interaction between Trigonelline and Humen Serum Albumin by Fluorescence Quenching Method[J].Acta Chinese Medicine and Pharmacology,2010,38(6):57-59.
Authors:WU Wen-hua  Zhao Yan  Cao Yi  HAN Feng-mei  CHEN Yong
Institution:(Hubei Provincial Key Lab of Bio-Technology of Chinese Medicine,Hubei University,Wuhan 430062,China)
Abstract:Objective: To investigate the effect of trigonelline on human serum albumin(HSA).Methods: The experiment compared the interactions from different concentrations of trigonelline to human serum albumin(HSA) by means of the fluorescence quenching under the conditions of pH 7.4 and 286nm excitation wavelength.Results: When the temperature were 37℃ and 47℃,the binding constant K between trigonelline and HSA were 749.03L·mol-1 and 106.29L·mol-1 with the binding sites(n) value of 1.0077and 0.7625,respectively.Conclusion: The results showed that trigonelline had a ability but not intensively to quench the fluorescence of humen serum albumin(HSA),and when the reaction temperature is increased,negative effects appear on the binding reaction.The changes of the thermodynamic parameters of binding interaction at 37℃ and 47℃ indicated that the main binding force between trigonelline and humen serum albumin was electrostatic force.
Keywords:Trigonelline  Humen serum albumin  Fluorescence quenching
本文献已被 CNKI 维普 万方数据 等数据库收录!
设为首页 | 免责声明 | 关于勤云 | 加入收藏

Copyright©北京勤云科技发展有限公司  京ICP备09084417号