I-125-LABELED PEPTIDE-MAPPING OF PROTEIN-III ISOLATED FROM 4 STRAINS OF NEISSERIA-GONORRHOEAE
I-125-LABELED PEPTIDE-MAPPING OF PROTEIN-III ISOLATED FROM 4 STRAINS OF NEISSERIA-GONORRHOEAE
复制标题
DOI：
10.1128/iai.37.2.622-631.1982
复制
发表时间：
1982-01-01
影响因子：
3.1
通讯作者：
JUDD, RC
中科院分区：
文献类型：
--
作者：
JUDD, RC
采用十二烷基硫酸钠-聚丙烯酰胺凝胶电泳技术，从4株非毛状（P-）透明（O-）淋球菌全细胞和外膜裂解物中分离出淋球菌外膜蛋白I （PI）和PIII。这些蛋白经放射性碘化处理后，用α -凝乳胰蛋白酶消化。然后用高压薄层电泳分离所得的125i肽，然后用上升薄层色谱和放射自显影。结果证实了先前关于PI具有不同表观亚基分子量的结构关系的观察结果。所有PIII都具有非常相似的表观初级结构，无论它们是从哪个菌株分离出来的，来源（即全细胞或外膜），或十二烷基硫酸钠裂解物的还原状态。通过使用的技术，似乎PIII在所有淋球菌菌株中结构相似，即使每个菌株具有结构独特的PI。
Gonococcal outer-membrane protein I (PI) and PIII were isolated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis from reduced and unreduced whole-cell and outer-membrane lysates of 4 strains of nonpiliated (P-), transparent (O-) N. gonorrhoeae. These proteins were radioiodinated and digested with .alpha.-chymotrypsin. The resultant 125I-peptides were then resolved by high-voltage thin-layer electrophoresis, followed by ascending TLC and visualized by autoradiography. Results corroborated previous observations regarding the structural relationships of PI having different apparent subunit MW. All PIII had very similar apparent primary structures, regardless of the strain from which they were isolated, the source (i.e., whole cells or outer membranes), or the reduction state of the sodium dodecyl sulfate lysates. By the techniques used, it appeared that PIII is structurally similar in all of the gonococcal strains, even though each strain had structurally unique PI.