蛋白质与表面活性剂相互作用的导数紫外光谱

The Derivative Ultraviolet Spectroscopy in the Process of the Interaction Between Protein and Surfactant

利用四阶导数紫外光谱法研究了在pH=7.40,离子强度I=0.0131mol·L-1的磷酸盐缓冲溶液中,浓度为1.0g·L-1的牛血清白蛋白(BSA)与十二烷基硫酸钠(SD S)相互作用的过程中,芳香族氨基酸残基微环境极性的变化。通过研究发现,随着SDS浓度的不断增大,三种芳香族氨基酸残基微环境极性的变化趋势不同,从而可以判断BSA与SDS相互作用过程中BSA构象的变化。

The variation of the micro-environmental polarity of aromatic amino acid residues in the process of the interaction of bovine serum albumin （BSA） with sodium dodecyl sulfate （SDS） under the experimental conditions of phosphate buffer at pH 7.40,maintaining the ionic strength of the overall solution at I=0. 0131mol·L-1 and the concentration of BSA at 1.0g·L-1,have been studied by fourth-derivative ultraviolet spectroscopy. The results showed that the micro-environmental polarity of the three aromatic amino acid residues varied differently when the concentration of SDS increased. The changes of the conformation of BSA were determined according to the variation of the micro-environmental polarity of these amino acid residues.