摘要
在酸性介质中,偶氮胭脂红B(ABX)与蛋白质在室温下能迅速结合生成复合物,其最大吸收波长为570 nm,比ABX红移了50 nm.本文用光度法研究了该结合反应的最佳条件,并在此基础上建立了一个测定蛋白质的新方法.在570 nm处各蛋白质的浓度至少在2.5～120 mg/L范围内与吸光度成正比,对测定牛血清蛋白质(BSA)、人血清蛋白(HSA)及γ-球蛋白(IgG)的桑德尔灵敏度分别为0.173、0.173和0.199 μg/cm2.除阴阳离子表面活性剂外,其余大部分物质不干扰蛋白质的测定.可见方法具有选择性好、灵敏度高且快速、稳定的优点,用于尿液及人血清样品中总蛋白的测定,所得结果与考马斯亮蓝方法测得结果基本一致.
In the acidic medium, azocarmine B (ABX) can bind rapidly with protein at room temperature forming a complex, which has a maximum absorption wavelength at 570 nm, and exhibits a bathochromic shift of 50 nm compared with the maximum absorption wavelength of ABX. The optimum reaction conditions were investigated, and a new method for the determination of proteins was developed based on this binding reaction. The absorbance of the binding system at 570 nm is proportional to the concentration of some proteins in the range of 2.5 similar to 120 mg/L with a sensitivity of 0.173, 0.173 and 0.199 mug/cm(2) for the determination of bovine serum albumin (BSA), human serum albumin (HSA) and human immunoglobulin G (IgG), respectively. A lot of the foreign substances do not interfere is the determination except for the anionic surfactant and cationic surfactant. The proposed method, which is rapid, stable, and of good selectivity and high sensitivity, has been used for the determination of the total protein in urine and human serum samples. The results obtained by this method agreed well with those obtained by Coomassie brillant blue G-250 method.
出处
《分析化学》
SCIE
EI
CAS
CSCD
北大核心
2002年第2期222-226,共5页
Chinese Journal of Analytical Chemistry
基金
云南省教委基金资助项目(No.00l2084)
