引用本文:
迟燕华, 庄稼, 毕欣颖, 周磊. 二乙基巴比妥酸与牛血清白蛋白相互作用的荧光光谱法[J]. 应用化学,
2007, 24(10): 1167-1171.
Citation: CHI Yan-Hua, ZHUANG Jia, BI Xin-Ying, ZHOU Lei. Interaction of Diethylmalonylurea and Bovine Serum Albumin Studied by Fluorescence Method[J]. Chinese Journal of Applied Chemistry, 2007, 24(10): 1167-1171.
Citation: CHI Yan-Hua, ZHUANG Jia, BI Xin-Ying, ZHOU Lei. Interaction of Diethylmalonylurea and Bovine Serum Albumin Studied by Fluorescence Method[J]. Chinese Journal of Applied Chemistry, 2007, 24(10): 1167-1171.
二乙基巴比妥酸与牛血清白蛋白相互作用的荧光光谱法
摘要:
采用荧光光谱法、紫外-可见光谱法研究了二乙基巴比妥酸(BBT)与牛血清白蛋白(BSA)的相互作用机理。结果发现,BBT对BSA有较强的荧光猝灭作用,分别在17和37℃时,根据荧光猝灭数据,由Stern-Volmer方程求得动态猝灭常数17℃KSV=1.427×104和37℃KSV=1.195×104,由Lineweaver-Burk双倒数方程得到了静态猝灭常数17℃KLB=9.848×103和37℃KLB=1.778×103。获得反应的结合常数K0=4.341×104,推导出结合位点数n=1.136和ΔH、ΔS和ΔG等热力学参数。说明了温度升高有利于BBT-BSA的结合作用的反应。并由此推出了结合反应的主要作用力类型。利用同步荧光技术,研究了BBT对BSA构象的影响。
English
Interaction of Diethylmalonylurea and Bovine Serum Albumin Studied by Fluorescence Method
Abstract:
The interaction mechanism of diethylmalonylurea(BBT) with bovine serum albumin(BSA) was studied by fluorescence and UV-Vis spectra. It is shown that BBT has a powerful ability to quench the fluorescence intensity of BSA. The fluorescence quenching data were analyzed according to Stern-Volmer equation and Line weaver-Burk equation at 17℃ and 37℃ to obtain the quenching constants, 17℃KSV=1.427×104 and 37℃KSV=1.195×104, 17℃KLB=9.848×103 and 37℃KLB=1.778×103, and the binding constant K0=4.341×104, and the thermodynamic parameters(ΔH, ΔS and ΔG). It was deduced that combining site n was 1.136. The increasing of temperature was favorable for the BBT-BSA interaction. According to the thermodynamic parameters, the major binding forces were determined. The effect of BBT on the conformation of BSA was analyzed Via synchronous fluorescence spectroscopy.
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