摘要
利用光吸收和共振光散射(RLS)光谱研究了铝试剂(ATA)与蛋白质在水溶液中的相互作用.在pH2.50时,蛋白质可使弱的ATA光散射信号曾强.基于这种现象,我们运用RLS技术,建立了测定纳克级蛋白质的方法.该方法简单、实用、灵敏.BSA的线性范围为0.010-27.4μg/mL,HSA的线性范围为0.010-30.5μg/mL.BSA的检测限为10.7ng/mL,HSA的检测限为10.2ng/mL.对实际人血清样品中的蛋白质进行了测定,其结果与临床方法一致.氨基酸、金属离子或其它共存化合物的干扰很小.
The interaction of the Indophenol Blue (ATA) with proteins in aqueous solution has been studied by optical absorption and Rayleigh Light Scattering (RLS) spectra. At pH 2.5, the weak RLS of ATA can be enhanced by the addition of proteins. Based on this, a novel method for the determination of proteins at nanogram levels by using RLS technique has been developed. Under optimum conditions, the linear range is 0.010- 27.4μg/mL for bovine serum albumin (BSA) and 0.010 - 30.5μLg/mL for human serum albumin (HSA). The method is simple, practical and much more sensitive, and it has been applied to the determination of proteins in human serum sampies, the results are very close to those provided by clinical physicians. There is very little interference from amino acids, metal ions and other coexisting compounds.
出处
《淮阴师范学院学报(自然科学版)》
CAS
2006年第2期135-139,共5页
Journal of Huaiyin Teachers College;Natural Science Edition
基金
江苏省教育厅自然科学基金资助项目(04KJB150016)
江苏省低维材料化学重点建设实验室开放课题项目(JSKC06029)
关键词
共振光散射
铝试剂
蛋白质
测定
resonance light scattering
aluminon
protein
determination