Rosengren J, Hjertén S
J Chromatogr. 1977 Jan 21;131:99-108. doi: 10.1016/s0021-9673(00)80924-3.
In the presence of different neutral salts in high concentrations (ionic strength 1-3 M), pentyl-Sepharose was saturated with human serum albumin, and decyl-Sepharose with ovalbumin and phycoerythrin; the amount of protein bound to the adsorbent was taken as a measure of the hydrophobic interaction. The effects of the different ions on the adsorption of protein could, with one exception, be arranged according to the Hofmeister series. As the adsorption might also be influenced by alterations in the protein conformation, caused by the neutral salts, the proteins were studied by circular dichroism. Circular-dichroism spectra showed that 3 M sodium bromide and 3 M sodium thiocyanate changed the conformation of human serum albumin and ovalbumin, whereas 3 M sodium chloride and 1 M sodium sulphate did not. The conformational changes observed with sodium bromide and thiocyanate were accompanied by decreasing protein-adsorbent interaction, except for ovalbumin in 3 M sodium thiocyanate.
在高浓度（离子强度1 - 3M）的不同中性盐存在下，戊基琼脂糖用人类血清白蛋白饱和，癸基琼脂糖用卵清蛋白和藻红蛋白饱和；结合到吸附剂上的蛋白量被用作疏水相互作用的一种度量。除了一个例外，不同离子对蛋白质吸附的影响可以按照霍夫迈斯特序列排列。由于吸附也可能受到中性盐引起的蛋白质构象变化的影响，通过圆二色性对蛋白质进行了研究。圆二色性光谱表明，3M溴化钠和3M硫氰酸钠改变了人类血清白蛋白和卵清蛋白的构象，而3M氯化钠和1M硫酸钠则没有。除了在3M硫氰酸钠中的卵清蛋白外，观察到的溴化钠和硫氰酸钠引起的构象变化伴随着蛋白质 - 吸附剂相互作用的降低。
