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采用荧光光谱法研究了不同酸度下,2-硝基苯胺与牛血清白蛋白(BSA)间的相互作用。实验结果表明,2-硝基苯胺对BSA的猝灭机制属于静态猝灭过程。经研究得到了不同酸度和不同温度下2-硝基苯胺与BSA反应的结合常数、结合位点数。根据热力学常数确定了二者间的作用力类型为氢键和疏水作用力。同步荧光结果表明,2-二硝基苯胺的存在改变了牛血清白蛋白的分子构象。
Fluorescence spectroscopy was used to study the interaction between 2-nitroaniline and bovine serum albumin (BSA) under different acidity. The experimental results show that the quenching mechanism of 2-nitroaniline to BSA belongs to the static quenching process. The binding constants and binding sites of 2-nitroaniline with BSA at different acidities and temperatures were obtained. According to the thermodynamic constants, the type of interaction between the two is determined as hydrogen bond and hydrophobic force. Synchronous fluorescence results show that the presence of 2-dinitroaniline alters the molecular conformation of bovine serum albumin.