Basch J J, Farrell H M
Biochim Biophys Acta. 1979 Mar 27;577(1):125-31. doi: 10.1016/0005-2795(79)90014-x.
Globular proteins, casein, and membrane proteins which were reacted with sodium dodecyl sulfate were studied by acid urea gel electrophoresis. The sodium dodecyl sulfate bound tightly to the proteins, producing a more acidic charge which prevented migration into the gel. When cetyltrimethylammonium bromide was added to the sodium dodecyl sulfate-protein complexes, the sodium dodecyl sulfate apparently reacted with cetyltrimethylammonium bromide and dissociated so that the proteins migrated in acid gel in a normal manner as compared to the proteins without any added detergent. The sodium dodecyl sulfate-cetyltrimethylammonium bromide complex could be removed from the proteins by centrifugation. Thus, cetyltrimethylammonium bromide used in conjunction with acid gel electrophoresis allows direct comparison by charge of proteins fractionated in the presence of sodium dodecyl sulfate with the starting mixture of proteins not exposed to detergent. The reaction of cetyltrimethylammonium bromide with sodium dodecyl sulfate in acidic urea also provides a simple convenient method of removal of sodium dodecyl sulfate from proteins.
通过酸性尿素凝胶电泳研究了与十二烷基硫酸钠反应的球状蛋白质、酪蛋白和膜蛋白。十二烷基硫酸钠与蛋白质紧密结合，产生更多酸性电荷，从而阻止其向凝胶中迁移。当将十六烷基三甲基溴化铵添加到十二烷基硫酸钠 - 蛋白质复合物中时，十二烷基硫酸钠显然与十六烷基三甲基溴化铵发生反应并解离，使得蛋白质在酸性凝胶中以正常方式迁移，这与未添加任何去污剂的蛋白质相比。通过离心可以从蛋白质中去除十二烷基硫酸钠 - 十六烷基三甲基溴化铵复合物。因此，与酸性凝胶电泳结合使用的十六烷基三甲基溴化铵能够直接比较在十二烷基硫酸钠存在下分级分离的蛋白质与未接触去污剂的起始蛋白质混合物的电荷。十六烷基三甲基溴化铵与酸性尿素中的十二烷基硫酸钠的反应还提供了一种从蛋白质中去除十二烷基硫酸钠的简单便捷方法。
