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甲草胺与牛血清白蛋白相互作用的光谱法研究
引用本文:李文波,高松,张华新. 甲草胺与牛血清白蛋白相互作用的光谱法研究[J]. 化学与生物工程, 2011, 28(1): 7-9. DOI: 10.3969/j.issn.1672-5425.2011.01.003
作者姓名:李文波  高松  张华新
作者单位:荆楚理工学院化工与药学院,湖北,荆门,448000
基金项目:湖北省教育厅科学技术研究项目,荆楚理工学院科技项目
摘    要:在模拟人体生理条件下,采用分子光谱法研究了甲草胺与牛血清白蛋白的相互作用.结果发现,甲草胺对牛血清白蛋白的内源荧光有一定的猝灭作用,由Stern-Volmet方程和Van't Hoff等压方程分析和处理实验数据,得到了结合作用的平衡常数、结合反应的热力学参数,确定甲草胺与牛血清白蛋白主要依靠疏水作用力进行结合,该结合反...

关 键 词:甲草胺  牛血清白蛋白  荧光光谱法  热力学参数

Spectroscopic Studies on the Interaction of Alachlor to Bovine Serum Albumin
LI Wen-bo,GAO Song,ZHANG Hua-xin. Spectroscopic Studies on the Interaction of Alachlor to Bovine Serum Albumin[J]. Chemistry & Bioengineering, 2011, 28(1): 7-9. DOI: 10.3969/j.issn.1672-5425.2011.01.003
Authors:LI Wen-bo  GAO Song  ZHANG Hua-xin
Affiliation:(College of Chemical and Pharmaceutical Engineering,Jingchu University of Technology,Jingmen 448000,China)
Abstract:The interaction of alachlor to bovine serum albumin(BSA)was studied using molecular spectroscopy by imitating physiologic environment.It was shown that this compound had a powerful ability to quench the BSA fluorescence.By analyzing the spectral data with Stern-Volmer equation and Van’t Hoff equation,the static fluorescence quenching binding constant and the thermodynamic parameters were obtained.It was verified that the binding of alachor to BSA was maily due to hydrophobic interaction,which led to the fluorescence quenching.The binding reaction was spontaneous.Meanwhile,the action of alachlor made a certain effect on the secondary structure of BSA.
Keywords:alachlor  bovine serum albumin  fluorescence spectrum  thermodynamic parameter
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