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番茄红素与牛血清白蛋白的相互作用
引用本文:白梅竹,李红亮,张林雅.番茄红素与牛血清白蛋白的相互作用[J].光谱实验室,2012,29(2):668-671.
作者姓名:白梅竹  李红亮  张林雅
作者单位:中国计量学院生命科学学院,杭州市下沙高教园区学源街258号,310018
基金项目:国家自然科学基金资助项目(30900163);浙江省自然科学基金资助项目(Y307597)
摘    要:采用荧光光谱法研究了番茄红素(Lycopene)与牛血清白蛋白(BSA)的相互作用关系。研究表明,番茄红素能使BSA在340nm(λem)处产生荧光猝灭,猝灭机理为静态猝灭。pH=7.4,温度为293K时,猝灭时表观结合常数KA为5.33×104L.mol-1,结合位点数n为0.6461,同时荧光猝灭最大速率常数Kq=2.76×1012L.mol-1.s-1。二者呈自发结合且主要作用力为氢键和范德华力,结合距离r与能量转移效率E分别为5.6nm和0.098,偏酸性或碱性的条件使番茄红素与BSA的结合常数增加。

关 键 词:番茄红素  牛血清白蛋白  荧光光谱法  静态猝灭  结合作用力

Interaction of Lycopene with BSA
BAI Mei-Zhu , LI Hong-Liang , ZHANG Lin-Ya.Interaction of Lycopene with BSA[J].Chinese Journal of Spectroscopy Laboratory,2012,29(2):668-671.
Authors:BAI Mei-Zhu  LI Hong-Liang  ZHANG Lin-Ya
Affiliation:BAIMei-Zhu LIHong-Liang ZHANGLin-Ya(College of Life Sciences,China Jiliang University,Hangzhou 310018,P.R.China)
Abstract:The interaction of lycopene with bovine serum albumin(BSA) was studied by fluorescence spectrometry.The lycopene can quench the fluorescence of BSA at 340nm(λem) by static quenching mechanism.The apparent association constant KA was 5.33×104L·mol-1 while the number binding sites n was 0.6461 at 293K under pH value of 7.4,meanwhile the maximum speed constant Kq was 2.76×1012L·mol-1·s-1.Thermodynamic analysis showed that the binding between them was spontaneous,and hydrogen bond and Van Der Waals force were the predominant intermolecular force.The binding distance r and energy-transfer efficiency E were respectively 5.6nm and 0.098.Furthermore,the binding constant of lycopene with BSA increased under partial acid and alkalinity conditions.
Keywords:Lycopene  BSA  Fluorescence Spectroscopy  Static Quenching  Binding Interaction Force
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