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淋球菌外膜某些热可修饰蛋白的125I标记肽图谱分析

125I-labeled peptide mapping of some heat-modifiable proteins of the gonococcal outer membrane.

作者信息

Swanson J

出版信息

Infect Immun. 1980 Apr;28(1):54-64. doi: 10.1128/iai.28.1.54-64.1980.

Abstract

Gonococci from opaque colonies have cell wall outer membrane proteins that are lacking from organisms which form transparent colonies. These "colony opacity-associated" proteins are among a group of "minor" proteins that exhibit heat modification of their apparent subunit molecular sizes, are easily extracted by deoxycholate, have apparent subunit molecular weights varying from 24,000 to 29,000 and are exposed on the surfaces of gonococci. Other minor proteins found on gonococci are the "leukocyte association proteins," whose presence correlates with reactivities of gonococci with human neutrophils. Several of the colony opacity-associated proteins and leukocyte association proteins were subjected to 125I-peptide mapping of protein bands separated by polyacrylamide electrophoresis in the presence of sodium dodecyl sulfate. The structural similarities and differences among these heat-modifiable surface proteins were studied, as well as their similarities with the major protein of the gonococcal outer membrane. A relatively high apparent degree of structural homology is found among the heat-modifiable proteins from different strains of opaque colony gonococcal forms. There is also some apparent structural homology for 125I-peptides of heat-modifiable versus major proteins of the gonococcal outer membrane.

摘要

来自不透明菌落的淋球菌具有细胞壁外膜蛋白,而形成透明菌落的菌株则缺乏这些蛋白。这些“菌落不透明相关”蛋白属于一组“次要”蛋白,它们的表观亚基分子大小呈现热修饰,很容易被脱氧胆酸盐提取,表观亚基分子量在24,000至29,000之间,且暴露于淋球菌表面。在淋球菌上发现的其他次要蛋白是“白细胞关联蛋白”,其存在与淋球菌与人中性粒细胞的反应性相关。在十二烷基硫酸钠存在下,通过聚丙烯酰胺电泳分离的蛋白条带对几种菌落不透明相关蛋白和白细胞关联蛋白进行了¹²⁵I-肽图谱分析。研究了这些热修饰表面蛋白之间的结构异同,以及它们与淋球菌外膜主要蛋白的相似性。在不同菌株的不透明菌落淋球菌形式的热修饰蛋白之间发现了相对较高的表观结构同源程度。淋球菌外膜的热修饰蛋白与主要蛋白的¹²⁵I-肽之间也存在一些明显的结构同源性。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/306c/550893/1032e067a721/iai00172-0068-a.jpg

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