Heckels J E
J Bacteriol. 1981 Feb;145(2):736-42. doi: 10.1128/jb.145.2.736-742.1981.
Outer membranes from opaque colonia variants of Neisseria gonorrhoeae P9 contain a major outer membrane protein (protein I) together with one or more of a series of heat-modifiable proteins (proteins II). Proteins I. II, and IIa have been isolated by detergent extraction of outer membranes. Amino acid analysis showed proteins II and IIa to have a very similar composition. Cyanogen bromide cleavage of proteins II and IIa produced a pair of fragments with identical molecular weight and a pari which differed by an amount (0.5K) equivalent to the difference between the intact proteins. Tryptic peptide maps of 125I-labeled proteins II, IIa, and IIb showed many similarities, with only a few peptides unique to any one protein. Peptide maps of protein IIa from cells which had been surface labeled showed that the unique peptides were exposed on the surface. The heat-modifiable proteins thus appear to form a family of proteins with closely related structure probably differing in that part which is exposed on the bacterial surface.
淋病奈瑟菌P9不透明菌落变体的外膜含有一种主要外膜蛋白(蛋白I)以及一系列热可变蛋白(蛋白II)中的一种或多种。通过用去污剂提取外膜已分离出蛋白I、II和IIa。氨基酸分析表明蛋白II和IIa具有非常相似的组成。蛋白II和IIa经溴化氰裂解产生一对分子量相同的片段和一对相差相当于完整蛋白之间差异量(0.5K)的片段。125I标记的蛋白II、IIa和IIb的胰蛋白酶肽图显示出许多相似之处,只有少数肽是任何一种蛋白所特有的。来自经表面标记的细胞的蛋白IIa的肽图表明,这些独特的肽暴露在表面。因此,热可变蛋白似乎形成了一个结构密切相关的蛋白家族,可能在暴露于细菌表面的部分有所不同。