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利用荧光光谱法和紫外光谱法研究了模拟生理条件下N-丁基-N’-(对氨基苯磺酸钠)硫脲(BPT)与人血清白蛋白(HSA)的相互作用。研究结果表明,BPT对HSA内源荧光的猝灭是静态猝灭。由热力学参数确定了BPT与HSA间存在疏水作用,根据Frster能量转移理论计算出结合距离为2.97 nm。通过三维荧光光谱研究了BPT对HSA构象的影响。在二者相互作用的基础上,以BPT为分子探针,运用同步荧光光谱法测定了生物样品中的蛋白质含量。对人血清、唾液和尿样进行平行测定并进行加标回收实验,回收率在96.2%～101.9%之间。
The interaction between N-butyl-N ’- (sodium p-aminobenzenesulfonate) thiourea (BPT) and human serum albumin (HSA) under simulated physiological conditions was studied by fluorescence spectroscopy and ultraviolet spectroscopy. The results show that the quenching of endogenous fluorescence of HSA by BPT is static quenching. The hydrophobic interaction between BPT and HSA was confirmed by the thermodynamic parameters, and the binding distance was calculated to be 2.97 nm according to Frster energy transfer theory. The effect of BPT on the conformation of HSA was studied by three-dimensional fluorescence spectroscopy. Based on the interaction between them, BPT was used as a molecular probe to determine the protein content in biological samples by synchronous fluorescence spectrometry. Parallel determination of human serum, saliva and urine samples and spike recovery experiments showed that the recoveries ranged from 96.2% to 101.9%.