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光谱法研究丙烯酰胺与牛血清白蛋白的相互作用
引用本文:鞠鹏,范海,吴晓娜,艾仕云,刘涛,崔琳.光谱法研究丙烯酰胺与牛血清白蛋白的相互作用[J].山东农业大学学报(自然科学版),2011,42(4):477-482.
作者姓名:鞠鹏  范海  吴晓娜  艾仕云  刘涛  崔琳
作者单位:山东农业大学化学与材料科学学院,山东泰安,271018
基金项目:国家自然科学基金项目(21075078); 山东省自然科学基金项目(ZR2010BM005)
摘    要:本文从光谱学的角度研究了有毒物质丙烯酰胺(AA)与牛血清白蛋白(BSA)间的相互作用.实验结果表明,在pH =7.0和室温条件下,AA可通过静态猝灭的方式有效地猝灭BSA的荧光,AA的加入影响了BSA的构象.通过荧光数据计算可得到AA与BSA的结合位点数(n=0.933)及表观绑定常数(KA=5.55×103 mol·...

关 键 词:丙烯酰胺  牛血清白蛋白  荧光猝灭  相互作用

A STUDY OF THE INTERACTION BETWEEN ACRYLAMIDE AND BOVINE SERUM ALBUMIN USING SPECTROSCOPY METHODS
JU Peng,FAN Hai,WU Xiao-na,AI Shi-yun,LIU Tao,CUI Lin.A STUDY OF THE INTERACTION BETWEEN ACRYLAMIDE AND BOVINE SERUM ALBUMIN USING SPECTROSCOPY METHODS[J].Journal of Shandong Agricultural University,2011,42(4):477-482.
Authors:JU Peng  FAN Hai  WU Xiao-na  AI Shi-yun  LIU Tao  CUI Lin
Institution:JU Peng,FAN Hai,WU Xiao-na,AI Shi-yun,LIU Tao,CUI Lin(College of Chemistry and Material Science,Shandong Agricultural University,Taian 271018,China)
Abstract:The interaction between acrylamide(AA) and bovine serum albumin(BSA) was studied mainly from a spectroscopic angle.Under pH 7.0,AA effectively quenched the intrinsic fluorescence of BSA via static quenching and conformational changes of BSA were observed.The number of binding sites(n = 0.933) and apparent binding constant(KA = 5.55 ×103 M-1) were calculated by relevant fluorescence data,and thus indicated the existence of just a single binding site in BSA for AA.According to the controlled experiments,the optimal reaction conditions were obtained as follows: the reaction time of 50 min,ionic strength of 0.05 mol·kg-1,and pH = 7.0.The effect of AA on the conformation of BSA can also be deduced by means of resonance scattering spectrum,UV-visible absorption spectrum and FT-IR measurement.Therefore,The binding study of AA with BSA is of great importance in the research of the effect of toxicity to biomolecules.
Keywords:Acrylamide(AA)  BSA  fluorescence quenching  interaction  
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