摘要
偶氮胭脂红G在酸性介质中与蛋白质迅速结合,生成一紫红色复合物,该复合物在570 nm处有最大吸收,且其吸光强度与牛血清蛋白(BSA)、人血清蛋白(HSA)、免疫球蛋白(IgG)的质量浓度至少在15.0μg/mL范围内有线性关系.依此建立的测定蛋白质的光度分析新方法不受蛋白酶和大部分其它共存物质的影响,具有较好的选择性和较宽的线性范围,同时方法快速、稳定,用于人血清样品中总蛋白含量的测定,所得结果与测定蛋白质的经典方法考马斯亮蓝G-250法基本一致.
A purple-red complex could be formed rapidly between azocarmine G and proteins in acidic medium. The absorbance of this complex at its maximum absorption wavelength of 570 nm increased linearly with the concentration of bovine serum albumin （BSA）, human serum albumin （HSA） and human Immunoglobulin G （IgG） at least in 15.0 μg/mL. Proteinase and the majority of other coexist substances did not interfere in the determination of protein by the new spectrophotometric method established according to this binding reaction between azocarmine G and proteins. The results obtained by this method, which was simple, rapid, selective and of wide determination range were agreed well with that obtained by Coomassie brillant blue G-250 method.
出处
《云南大学学报（自然科学版）》
CAS
CSCD
北大核心
2008年第1期83-86,共4页
Journal of Yunnan University(Natural Sciences Edition)
基金
云南省人才培引项目资助(2004PY01-4)
云南省高校教学、科研带头人项目资助
