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作 者:李燕[1] 宋桂兰[1] 卢燕[1] 杨兴[2] 魏琴[1]
机构地区:[1]济南大学化学化工学院,济南250022 [2]辽宁石油化工大学石油化工学院,抚顺113001
出 处:《分析试验室》2009年第3期55-58,共4页Chinese Journal of Analysis Laboratory
基 金:山东省重点学科基金(XTD0705)项目资助
摘 要:在pH2.21的B-R缓冲溶液中,蛋白质的加入导致荧光镓共振瑞利散射信号增强,基于此,建立了一种测定蛋白质的新方法。表面活性剂SDS的加入显著提高了体系的灵敏度,牛血清白蛋白的浓度在0~4.5μg/mL之间与体系的散射强度呈线性关系,检出限为8.14ng/mL。方法已应用于人血清样品中蛋白质含量的测定。同时,利用分光光度法测定了其不同温度下的结合数、结合常数。利用热力学方程研究发现荧光镓与蛋白质之间的主要作用力为静电引力。In pH 2.21 B-R buffer, the addition of protein enhanced the rayleigh light scattering of Lumogallion greatly. Based on this, a novel method for the determination of protein was developed. The sensitivity of the system was increased significantly after SDS was added. The scattering intensity of the system was proportional to the concentration of bovine serum albumin in the range of 0 -4.5 μg/mL and the detect limit was 8.14 ng/mL. The method developed in this paper has been used for the determination of protein in human serum albumin successfully. Meanwhile, the bind- ing number and binding constant under different temperatures were calculated by spectrophotometry. It is found that static electronic force plays an important role in the interaction between lumogallion and protein according to thermodynamic equation.
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