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作 者:李浩然[1] 张素娇[1] 乔媛媛[1] 周小纳[1] 秦伟明[1] 敖登高娃[1]
机构地区:[1]内蒙古大学化学化工学院,呼和浩特010021
出 处:《内蒙古大学学报(自然科学版)》2009年第4期438-442,共5页Journal of Inner Mongolia University:Natural Science Edition
基 金:内蒙古大学本科生创新基金
摘 要:在pH 4.80的HAc-NaAc缓冲液中,用溴邻苯三酚红(BPR)-Eu3+作为光谱探针,以Triton-100为胶束增敏剂,采用分光光度法研究了BPR-Eu3+-蛋白质三元离子缔合物的光谱性质及生成条件.牛血清白蛋白(BSA)浓度在3.35~60.3μg/mL范围内三元离子缔合物的吸光度遵循比尔定律,线性回归方程为:A=0.0485 c-0.0089(c:mol.L-1),相关系数R=0.9993,表观摩尔吸收系数为4.8×105L.mol-1.cm-1.初步探讨了其反应机理,BSA与BPR-Eu3+络合物之间主要以静电引力相结合.用该方法对生物样品中蛋白含量进行测定,结果满意.In the medium of a buffer solution of HAc-NaAc (pH 4.80),the spectra characteristic and association condition of ion-association complex of BPR-Eu^3+-BSA were studied with bromopyrogallol red and europium complex as the spectral probe and Triton-100 as a micellar strengthen reagent. The results show that the concentration of BSA and absorbency obeyed the Beer's law in the range of 3.35~60.3μg/mL and the regression equation was established as A=0.0485c-0.0089(c:mol·L^-1) with correlation coefficient R as 0. 9993, the apparent molar absorptivity was 4.8×10^5L·mol^-1·cm^-1. Preliminary study on the reaction mechanism shows that the main interaction was electrostatic attraction. This method was successfully applied to the analysis of proteins in biological sample ,and the results were satisfactory.
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