Cross-linking analysis of Neisseria gonorrhoeae outer membrane proteins.
The arrangement of proteins in the outer membrane of Neisseria gonorrhoeae was investigated through the use of cleavable chemical cross-linking reagents and two-dimensional sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Cross-linking of isolated outer membranes yielded dimers and trimers of the major outer membrane protein. In addition, data were obtained suggesting that a stable interaction exists between the major protein I and protein II, the second most prevalent protein in the gonococcal outer membrane.
D001426:Bacterial Proteins / Q000032:analysis*; D003432:Cross-Linking Reagents; D004591:Electrophoresis, Polyacrylamide Gel; D008565:Membrane Proteins / Q000032:analysis*; D009344:Neisseria gonorrhoeae / Q000032:analysis*
D001426:Bacterial Proteins; D003432:Cross-Linking Reagents; D008565:Membrane Proteins