中文摘要：

采用摇床法,测定25℃不同浓度硫酸铵时变性牛胰核糖核酸酶（RNase A）在固体疏水作用色谱填料PEG-600表面上的吸附等温线.得出随盐浓度的增加,变性蛋白分子与疏水表面吸附亲和作用增强,吸附量随盐浓度的增加而增大.DSC和FTIR的研究证实,变性吸附态蛋白分子的热稳定性随盐浓度的增加而增强,保留了更多的蛋白二级结构,且在疏水表面上进行再折叠,得到部分有序的蛋白三级结构.

英文摘要：

By varying concentrations of ammonium sulfate in solutions,adsorption isotherms of denatured（by 1.8 mol·L-1 guanidine hydrochloride） Ribonuclease A（RNase A）adsorbed by moderately hydrophobic pickings PEG-600 surface at 25℃ were determined.With salt concentration increment,the adsorption affinity of denatured protein molecules onto the hydrophobic surface increases and ordered conformation gained of adsorbed protein molecules enhances.Differential scanning calorimetry（DSC） and Fourier transform infrared spectroscopy （FUR） investigations confirmed that thermal stability of the adsorbed protein molecules increases and more secondary structures retain with increasing salt concentration. It was also found that partial tertiary structure of protein molecules may be gained as the denatured protein molecules refold on the hydrophobic surface.