【摘要】 用分光光度法研究了偶氮氯膦-mA-铌配合物与牛血清白蛋白(BSA)结合反应体系。在pH 3.0的磷酸氢二钠-柠檬酸缓冲溶液(Mcllvaine)中,随着BSA量的增加,偶氮氯膦mA-铌配合物在542 nm波长处吸收峰也随着减小。据此建立了以偶氮氯膦mA-铌配合物为光谱探针,光度法测定蛋白质的新方法。牛血清白蛋白量在0~60 mg/L范围内与体系的褪色程度呈良好的线性关系,其相关系数为r=0.9996,摩尔吸光系数为5ε42=3.3×105L.mol-1.cm-1。方法应用于人血清蛋白的测定。更多还原

【Abstract】 The interaction between CPA-mA-Nb(Ⅴ) and bovine serum albumin(BSA) was investigated.In a pH=3.0(Mcllvaine) buffer solution,with the increase of BSA concentration,the absorption peak at 542 nm decreased strikingly.The molar absorptivity is 3.35×105 L·mol-1·cm-1.Beer′s law was obeyed in a range from 0 to 60 mg/L.A spectrophotometric method for the determination of protein was established by using CPA-mA-Nb(Ⅴ) complex.The proposed method was applied to determination of albumin in human serum albumin and the results were in agreement with certified values.Recoveries of the standard addition for BSA were 98%～103% with RSD≤2.4%(n=6).更多还原