Cross-linking analysis of the outer membrane proteins of Neisseria gonorrhoeae.
AUTOR(ES)
Newhall, W J
RESUMO
The organization of outer membrane proteins of Neisseria gonorrhoeae was investigated by using two-dimensional dodecyl sulfate-polyacrylamide gel electrophoresis and cross-linking agents. A naturally occurring protein aggregate, which may be composed of two proteins of 50,000 molecular weight, was detected in all strains. Treatment of whole cells with cross-linking agents yielded several additional complexes, suggesting that other proteins are arranged in the outer membrane as near neighbors. The principal outer membrane protein (molecular weight, 34,000) cross-linked (i) to itself to form a complex whch appeared to be trimeric, (ii) to the 28,000-molecular-weight outer membrane protein to form a bimolecular comlex, and (iii) to the 28,000-molecular-weight outer membrane protein in a 3:1 ratio. The formation of these complexes was independent of (i) colony type, (ii) colony opacity, (iii) pH during growth, and (iv) presence of markers for drug resistance or hypersensitivity.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=551019Documentos Relacionados
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