中文摘要：

研究了钙红-Cu（Ⅱ）络合物与牛血清蛋白（BSA）作用的共振光散射光谱（RLS）、荧光光谱和电子吸收光谱特征，建立了利用金属配合物作为探针测定痕量蛋白质的方法。钙红-Cu（Ⅱ）-BSA三元络合物的形成导致RLS强度和荧光强度的增大；同时引起电子吸收光谱的强度减小，594nm处吸收峰消失。在pH5·65～5．75的酸度条件下，钙红-Cu（Ⅱ）络合物与BSA系统在317nm处有一增强的RLS光谱峰，且增强的RLS强度与BSA的浓度呈线性关系。在实验室确定的优化条件下，RLS强度与BSA浓度的线性范围为0.75～10μg·mL^-1，线性方程为I=150．88＋201．48c（BSA，μg·mL^-1），相关系数r=0．9973。方法检出限为5.62×10^-2μg·mL^-1。该方法成功地用于人工混合样品中BSA含量的测定。对钙红-Cu（Ⅱ）络合物与BSA的作用机制的研究表明，钙红-Cu（Ⅱ）络合物与BSA之间主要存在的是静电引力。

英文摘要：

The Resonance light scattering （RLS） spectra, fluorescence spectra, and absorption spectra of Cal-Red Cu（ Ⅱ ） metal complex with bovine serum albumin（BSA） were studied. As the Cal-Red-Cu（ Ⅱ ）-BSA complex formed, the RLS spectra and fluorescence spectra enhanced, but the absorption spectra weakened and the absorption peak at 594 nm disappeared. At pH 5.65-5.75, the enhanced RLS of CaPRed-Cu（ Ⅱ ） metal complex with BSA system was characterized by the maximum scattering at 317 nm, and the RLS intensity is proportional to the concentration of BSA. Under optimal conditions, the linear range of calibration was 0. 75-10 μg· mL^-1, the linear regression equation was I=150. 88＋201.48c（BSA, μg · mL^-1 ）with r=0. 997 3, and the limit of detection was 5.62×10^-2 μg·mL^-1. The method was applied to the determination of BSA in synthetic samples satisfactorily. A mechanism of electrostatic force was suggested for the interaction between BSA and Cal-Red Cu（ Ⅱ ）.