Paakkanen J, Gotschlich E C, Mäkelä P H
J Bacteriol. 1979 Sep;139(3):835-41. doi: 10.1128/jb.139.3.835-841.1979.
The protein composition of purified outer membranes of 47 Escherichia coli strains was examined by sodium dodecyl sulfate-polyacrylamide gradient gel electrophoresis. Of 33 encapsulated strains, all contained an outer membrane protein distinguishable from previously reported proteins. The 14 non-encapsulated strains with one exception lacked this protein. Because of its apparent association with encapsulation (K antigen) we have named it K protein. The protein was purified nearly to homogeneity by chromatography in the presence of detergents, and its composition was determined. Its amino acid composition does not differ significantly from that reported for protein I, another E. coli major outer membrane protein. Furthermore, the N-terminal amino acid sequence of protein K indicates that it is related to protein I.
通过十二烷基硫酸钠-聚丙烯酰胺梯度凝胶电泳对47株大肠杆菌纯化外膜的蛋白质组成进行了检测。在33株有荚膜的菌株中，所有菌株都含有一种与先前报道的蛋白质不同的外膜蛋白。14株无荚膜菌株中，除一株外均缺乏这种蛋白质。由于它明显与荚膜（K抗原）相关，我们将其命名为K蛋白。通过在去污剂存在下进行层析，该蛋白被纯化至几乎同质，并确定了其组成。它的氨基酸组成与另一种大肠杆菌主要外膜蛋白I的报道没有显著差异。此外，K蛋白的N端氨基酸序列表明它与蛋白I有关。
