ELECTROPHORETIC RESOLUTION OF MAJOR OUTER MEMBRANE PROTEIN OF ESCHERICHIA-COLI-K12 INTO 4 BANDS
ELECTROPHORETIC RESOLUTION OF MAJOR OUTER MEMBRANE PROTEIN OF ESCHERICHIA-COLI-K12 INTO 4 BANDS
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DOI：
10.1016/0014-5793(75)80272-9
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发表时间：
1975-01-01
期刊：
影响因子：
3.5
通讯作者：
VANALPHEN, L
中科院分区：
文献类型：
--
作者：
LUGTENBERG, B;MEIJERS, J;VANALPHEN, L
肠杆菌科的细胞被膜由两层膜组成，两层膜之间由肽聚糖层隔开。已经开发了将细胞质膜与外膜分离的方法[1，2]。大肠杆菌的外膜含有60%的包膜蛋白[1]。使用聚丙烯酰胺凝胶电泳，Schnaitman在外膜组分中发现了六条蛋白带，其中一条带（mol. wt 44 000）占总外膜蛋白的70%[11.这种蛋白质被称为“主要外膜蛋白”。Schnaitman最近报道，E.大肠杆菌0 111-B4菌株的蛋白质电泳图谱可分为3条不同的条带，分别命名为条带1、2和3。在E. coli K12 [3]。Henning等人[4]也发现E. coliK 12中分离到两条带，并报道了它们的分子量。WTS约。四万艾姆斯已成功地应用Laemmli [S]的凝胶电泳系统分离鼠伤寒沙门氏菌的主要包膜蛋白。而在E. cofi K12菌株HfrH，她仅发现两条主要条带，重量为29 000和33 000 [6]。Neville [7]描述的系统也解析了大肠杆菌的主要外膜蛋白。cob K12分为两条带[8]。本文描述了一种新的凝胶电泳系统，该系统能更好地分离大肠杆菌的主要外膜蛋白。coli K12中表达。“主要外膜蛋白”的名称是错误的-
The cell envelope of Enterobacteriaceae consists of two membranes separated by a peptidoglycan layer. Methods have been developed to separate the cytoplasmic membrane from the outer membrane [1, 2]. The outer membrane of Escherichia coli contains 60% of the envelope protein [l]. Using polyacrylamide gelelectrophoresis, Schnaitman found six protein bands in the outer membrane fraction, of which one band (mol. wt 44 000) accounted for 70% of the total outer membrane protein [11. This protein was referred to as the ‘major outer membrane protein’. Schnaitman recently reported that this major outer membrane protein of E. coli strain 0 111-B4 could be resolved into three distinct bands, designated as protein bands 1, 2 and 3. Only bands 1 and 3 were found in E. coli K12 [3]. Henning et al.[4] too found that the major protein of outer membrane preparations of E. coli K12 could be resolved into two bands, for which they reported mol. wts of approx. 40 000. Ames has applied the gelelectrophoresis system of Laemmli [S] very successfully for the separation of the major envelope protein of Salmonella typhimurium. However, in cell envelopes of E. cofi K12 strain HfrH she found only two major bands with mol. wts of 29 000 and 33 000 [6]. Also the system described by Neville [7] resolves the major outer membrane protein of E. cob K12 into two bands [8]. In this paper we describe a new gelelectrophoresis system which results in a better resolution of the major outer membrane protein of E. coli K12. The designation ‘major outer membrane protein’is mis-