Palva E T
Eur J Biochem. 1979 Feb 1;93(3):495-503. doi: 10.1111/j.1432-1033.1979.tb12848.x.
Specific protein interactions in Escherichia coli outer membrane were analyzed using chemical cross-linking with truly cleavable reagents and symmetrical two-dimensional sodium dodecyl sulphate/polyacrylamide gel electrophoresis. The major outer membrane proteins were shown to form cross-linked complexes. These include multimers of lambda receptor, protein I, II, III and the free form of lipoprotein. Lipoprotein was also found to be cross-linked to proteins II and III. The identity of many of these complexes was verified using appropriate mutants missing the proteins in question. No new protein interactions were detected in the mutants even when three of the major proteins were missing. Proteins II, III and the free form of lipoprotein could also be cross-linked to the peptidoglycan layer of the cell wall.
利用与真正可裂解试剂的化学交联以及对称二维十二烷基硫酸钠/聚丙烯酰胺凝胶电泳，分析了大肠杆菌外膜中的特异性蛋白质相互作用。结果表明，主要外膜蛋白形成了交联复合物。这些复合物包括λ受体、蛋白I、II、III的多聚体以及脂蛋白的游离形式。还发现脂蛋白与蛋白II和III发生了交联。使用缺失相关蛋白质的合适突变体验证了其中许多复合物的身份。即使缺失三种主要蛋白质，在突变体中也未检测到新的蛋白质相互作用。蛋白II、III和脂蛋白的游离形式也可与细胞壁的肽聚糖层发生交联。
