Ames G F, Spudich E N, Nikaido H
J Bacteriol. 1974 Feb;117(2):406-16. doi: 10.1128/jb.117.2.406-416.1974.
The protein composition of the outer membrane of Salmonella typhimurium has been analyzed by electrophoresis on slabs of sodium dodecyl sulfate-acrylamide gel. This powerful technique allows very high resolution of protein mixtures and has permitted the identification of multiple major protein components of the outer membrane; no evidence for a single major component of molecular weight 44,000 was obtained. These proteins were shown to be decreased in amount in mutants which have defective lipopolysaccharides. Mutants of an apparently new type were also found which contain decreased amounts of the proteins and the parent-like lipopolysaccharide, yet are resistant to a lipopolysaccharide-specific phage, C21. Several outer membrane proteins are insoluble in sodium dodecyl sulfate unless heated at high temperature (above 70 C). A purification procedure based on this property is tentatively suggested.
鼠伤寒沙门氏菌外膜的蛋白质组成已通过在十二烷基硫酸钠 - 丙烯酰胺凝胶平板上进行电泳分析。这种强大的技术能够对蛋白质混合物进行非常高分辨率的分析，并已鉴定出外膜的多种主要蛋白质成分；未获得分子量为44,000的单一主要成分的证据。这些蛋白质在脂多糖有缺陷的突变体中含量减少。还发现了一种显然新型的突变体，其蛋白质和类似亲本的脂多糖含量均降低，但对脂多糖特异性噬菌体C21具有抗性。几种外膜蛋白在十二烷基硫酸钠中不溶，除非在高温（70℃以上）下加热。初步提出了基于此特性的纯化程序。
