铬(Ⅵ)与蛋白质相互作用的共振瑞利散射光谱及其分析应用

Resonance Rayleigh Scattering Spectra of Chromium(Ⅵ)-Protein Systems and Their Analytical Application

在酸性介质中,重铬酸钾和某些白蛋白的共振瑞利散射(RRS)均十分微弱,但当两者相互作用形成结合产物时,将导致共振瑞利散射显著增强并出现新的RRS光谱。本研究考察了反应体系的RRS光谱特征、适宜的反应条件、影响因素及分析化学性质。不同蛋白质分别在0.2～50mg/L(HSA),0.5～60mg/L(OVA)和2.0～80mg/L(BSA)的浓度范围内与散射强度(ΔI)成正比。铬(Ⅵ)对人血清白蛋白的检出限为54.0μg/L,并且方法有较好的选择性。由此建立了一种用铬(Ⅵ)RRS法测定蛋白质的简便、快速的新方法。

In the medium of pH 2.5～3.2, proteins react with potassium dichromate to form the binding products. This results in a significant enhancement of the Resonance rayleigh scattering (RRS) intensity, and the corresponding RRS spectra appear. The characteristic of RRS spectra, the influencing factors and the ~optimum conditions of reaction were investigated. The intensities of RRS are directly proportional to the ~concentration of proteins in the range of 0.2～50.0 mg/L for human serum albumin (HSA), 0.5～60.0 ~mg/L for ovalbumin (OVA) and 2.0～80 mg/L for bovine serum albumin (BSA), respectively. The ~detection limit for HSA is 54.0 μg/L. The method has good selectivity, and a simple and fast method for the ~determination of proteins by RRS was developed.