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水飞蓟素与牛血清白蛋白相互作用的荧光光谱研究
引用本文:尚永辉,孙家娟,刘静. 水飞蓟素与牛血清白蛋白相互作用的荧光光谱研究[J]. 化学研究, 2011, 22(2): 1-3
作者姓名:尚永辉  孙家娟  刘静
作者单位:咸阳师范学院化学与化工系,陕西,咸阳,712000
基金项目:国家自然科学基金项目(20975081); 西北大学研究生交叉学科资助项目(07YJC09); 陕西省教育厅科研计划项目(2010JK899)
摘    要:采用同步荧光光谱技术研究了pH=7.40的Tris-HCl缓冲体系中水飞蓟素与牛血清白蛋白(BSA)的相互作用以及水飞蓟素对BSA构象的影响.结果表明,水飞蓟素对BSA的荧光猝灭过程为静态猝灭,结合热力学参数△rH∞=-45.21 kJ·mol-1,△rSm=-61.61 J·K-1·mol-1;据此可以推断,水飞蓟素...

关 键 词:水飞蓟素  牛血清白蛋白  相互作用  荧光光谱

Fluorescence spectrometric study of interaction between silymarin and bovine serum albumin
SHANG Yong-hui,SUN Jia-juan,LIU Jing. Fluorescence spectrometric study of interaction between silymarin and bovine serum albumin[J]. Chemical Research, 2011, 22(2): 1-3
Authors:SHANG Yong-hui  SUN Jia-juan  LIU Jing
Affiliation:SHANG Yong-hui,SUN Jia-juan,LIU Jing(Department of Chemistry & Chemical Engineering,Xianyang Normal College,Xianyang 712000,Shaanxi,China)
Abstract:The interaction between silymarin and bovine serum albumin(BSA) in physiological buffer solution(pH = 7.40) as well as the effect of silymarin on the conformation of BSA were studied by means of synchronous fluorescence spectrometry.It was found that silymarin quenched the fluorescence of BSA via a static quenching process,with thermodynamic parameters including enthalpy change(△rHm) and entropy change(△rSm) being-45.21 kJ·mol-1 and-61.61 J·K-1·mol-1,respectively.Thus it could be inferred that the interaction between silymarin and BSA was driven mainly by hydrogen bonding and Van der Waals forces,and the binding process was a spontaneous process.
Keywords:silymarin  bovine serum albumin  interaction  fluorescence spectrometry  
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