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作 者:魏琴[1] 李燕[1] 于海琴[1] 李乐义[1] 杜斌[1]
出 处:《分析化学》2005年第8期1175-1178,共4页Chinese Journal of Analytical Chemistry
基 金:国家自然科学基金(No.50373017);山东省自然科学基金(No.Y2004B11);山东省教育厅科技计划项目(No.03C5);济南大学博士重点基金(No.B0405)
摘 要:研究了偶氮羧Ⅰ-铽(Ⅲ) 与蛋白质的相互作用及其应用.在pH 1.20的HCl-KCl缓冲溶液中,蛋白质的加入使得偶氮羧Ⅰ-铽 (Ⅲ) 在510 nm 处的吸收峰峰值明显降低,且吸光度的变化与加入的蛋白质的浓度呈线性关系,于510 nm处测得摩尔吸光系数为ε=7.75×105L/(mol·cm)-1,牛血清白蛋白在0~55 mg/L范围内符合朗伯-比尔定律.将此方法用于尿样和奶粉中蛋白质的测定,结果令人满意.The interactions and applications of carboxyazo Ⅰ - Tb( Ⅲ ) complex and protein were studied by spectrophotometric method. At pH 1.20 HCl-KCl buffer solution, when protein was added, the height of absorption peak of carboxyazo Ⅰ - Tb( Ⅲ ) complex at 510 nm decreased. Moreover, the decrease of the absorption was proportional to the concentration of protein, and the apparent molar absorptivity of the carboxyazo Ⅰ - Tb( Ⅲ ) -bovine serum albumin was 7.75 × 10^5L·mol^ -1· cm^-1 Beer's law was obeyed in the range of 0-55 mg/L. Both the influence of reaction variables and the iterference of coexisting substance are studied.The proposed method has been applied to the determination of protein in urine and milk powder successfully.The recoveries are 96.5% - 103% and the standard relative deviations are less than 3.5%. In addition, the binding number was estimated by the graphic method of rosenthanl and molar ratio, and every bovine serum albumin (BSA) can bind 78 molecules of carboxyzao Ⅰ - Tb( Ⅲ ).
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