摘要
在ｐＨ１．０～２．０的 Ｃｌａｒｋ－ｌｕｂｓ缓冲溶液中，铬蓝 ＳＥ与蛋白质结合形成复合物，导致铬蓝 ＳＥ褪色。吸光度的降低与蛋白质浓度成正比，建立了测定多种蛋白质的分光光度分析法。不同蛋白质在０－５０ｍｇ／Ｌ至０～８０ｍｇ／Ｌ浓度范围内服从Ｂｅｅｒ定律，其表观摩尔吸光系数在 ８．４ × １０４～９．０ ×１０５Ｌ·ｍｏｌ－１·ｃｍ－１之间。以牛血清白蛋白为例研究了离子强度和共存物质的影响。本法简便、准确、灵敏、选择性和重现性好。应用于人血清样品中总蛋白质量的测定，结果满意。
A novel method has been described for the spectrophotometric determination of proteins, which was based on a fading reaction between chrome blue SE and proteins to form complexes in clark-lubs buffer at pH 1.0 similar to 2.0. The decrease of absorbance was proportional to the concentration of proteins. Beer's law is obeyed in the range from 0 similar to 50 mg/L to 0 similar to 80 mg/L on the different proteins. The reactions have highly sensitivities and their apparent molar absorptivities of fading reactions are between 8.0 x 10(4) L . mol(-1) . cm(-1) and 9.0 x 10(5) L . mol(-1) - cm(-1). Taking bovine serum albumin as an example, we studied the effects of ionic strength and some coexistent substances on the determination. The method is highly selective, rapid, simple and repeatable and has been applied to the determination of total amounts of proteins in human serum samples with satisfactory results.
出处
《分析化学》
SCIE
EI
CAS
CSCD
北大核心
2002年第1期42-45,共4页
Chinese Journal of Analytical Chemistry
