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达旦黄与牛血清白蛋白作用的光谱特性
引用本文:康旭珍,李建晴.达旦黄与牛血清白蛋白作用的光谱特性[J].河北大学学报(自然科学版),2008,28(6):629.
作者姓名:康旭珍  李建晴
作者单位:晋中学院,化学化工学院,山西,晋中,030600
摘    要:以达旦黄为探针,应用荧光及紫外光谱法研究达旦黄(TY)与牛血清白蛋白(BSA)分子间的结合反应,测定了不同温度下的结合常数和结合位点数.实验表明:TY对BSA内源荧光的猝灭机理为静态猝灭,作用力类型为疏水作用.根据Frster能量转移理论,求得不同温度(16 ,30 ,40 ℃)下的能量转移效率E分别为0.419 6,0.401 9,0.386 5,作用距离r分别为3.05,3.04,3.10 nm.BSA存在猝灭TY的荧光,以此为基础建立了测定BSA的方法,线性范围:3×10-7~2×10-5 mol/L,检出限:9.07×10-7 mol/L,相对标准偏差:RSD=1.7%.

关 键 词:达旦黄  牛血清白蛋白  荧光猝灭  

Study on the Interaction Between Thiazol Yellow G and Bovine Serum Albumin by Fluorescence
KANG Xu-zhen,LI Jian-qing.Study on the Interaction Between Thiazol Yellow G and Bovine Serum Albumin by Fluorescence[J].Journal of Hebei University (Natural Science Edition),2008,28(6):629.
Authors:KANG Xu-zhen  LI Jian-qing
Abstract:The interactions between thiazol yellow G(TY)and bovine serum albumin(BSA) were studied by fluorescence spectroscopy.The binding constants and binding sites of TY with BSA were measured at different temperatures.The experimental results revealed that TY has a strong ability to quench the intrinsic fluorescence of BSA and the interaction has been verified as consistent with the static quenching procedure.According to thermodynamic parameters,the acting forces were determined to be hydrophobic force.Based on the mechanism of the Frster energy transference,the transfer efficiency of energy E and transfer distance r between the acceptor TY and donor BSA were obtained at different temperatures(16,30,40 ℃).E = 0.419 6,r = 3.05 nm;E=0.401 9,r = 3.04 nm;E = 0.386 5,r = 3.10 nm respectively.The presence of BSA could decrease the fluorescence intensity of TY.And the F0/F was linear in the range(LDR)of 3×10-7~2×10-5 mol/L,the limit of detection(LOD) was 9.07×10-7 mol/L,and the relative standard deviation was 1.7%.
Keywords:thiazol yellow G  bovine serum albumin  fluorescence quenching
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