在pH 7.4的Tris-HCl缓冲溶液中,荧光猝灭光谱和三维荧光光谱显示磺胺嘧啶钠(SDS)可与人血清白蛋白(HSA)相互作用,使人血清白蛋白疏水微环境极性以及构象发生变化。考察了Δλ值、反应介质、离子强度等因素对该体系同步荧光光谱特征及强度的影响。在选定的最佳实验条件下,体系的同步荧光强度(ISF)与人血清白蛋白在1.38～276μg/mL的浓度范围内呈现良好的线性关系,线性相关系数为0.9992,从而建立了以磺胺嘧啶钠为分子探针,用固定波长同步荧光光谱分析测定蛋白质的新方法,检测限可达0.48μg/mL。用此方法对生物样品人血清、唾液和尿液中蛋白质含量进行了测定并进行加标回收实验,回收率在95.7%～103.7%之间。本文还用经典的考马斯亮蓝法对样品进行了测定,所得结果和本方法一致。同时还考察了一些常见的共存物质对蛋白质测定的影响。 Fluorescence quenching spectroscopy and three-dimensional fluorescence spectroscopy showed that sodium sulfadiazine (SDS) interacts with human serum albumin (HSA) in a pH 7.4 Tris-HCl buffer solution to render the hydrophobic microenvironment of human serum albumin polar and conformational Change. The effects of Δλ, reaction medium and ionic strength on the characteristics and intensity of synchronous fluorescence spectra of the system were investigated. Under the optimal experimental conditions, the syngeneic fluorescence intensity (ISF) showed a good linear relationship with the concentration of human serum albumin in the range of 1.38 ~ 276μg / mL with a linear correlation coefficient of 0.9992, Pyrimidine sodium as a molecular probe, using fixed wavelength synchronous fluorescence spectrometry for the determination of protein, a new detection limit of up to 0.48μg / mL. Using this method, the protein content in human serum, saliva and urine of biological samples was determined and the spiked recovery experiments were carried out. The recoveries ranged from 95.7% to 103.7%. In this paper, the samples were also measured by the classical Coomassie Brilliant Blue method, and the results are consistent with this method. Also examined some common coexisting substances on the determination of the impact of the protein.