Conservation of peptide structure of outer membrane protein-macromolecular complex from Neisseria gonorrhoeae.
AUTOR(ES)
Hansen, M V
RESUMO
The structural conservation of an outer membrane protein of Neisseria gonorrhoeae called OMP-MC (outer membrane protein-macromolecular complex) was investigated by determining the isoelectric point and amino-terminal amino acid sequence of the protein and by using high-performance liquid chromatography for comparative tryptic peptide mapping. The 76,000-dalton subunits generated by reduction and alkylation of the native 800,000-dalton complex from six test strains focused in ultrathin gels as bands of restricted heterogeneity at an approximate pI of 7.6. Dansyl chloride labeling indicated that all strains shared glycine as the amino-terminal amino acid. Sequence analysis of OMP-MC from two strains revealed no amino acid differences within the first 11 residues. Dual-label peptide maps revealed an extremely high degree of conservation of peptide structure. The results indicate that (i) OMP-MCs isolated from various strains of N. gonorrhoeae share structural homology and (ii) the 800,000-dalton complex is a homopolymer composed of 10 to 12 apparently identical 76,000-dalton subunits.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=264258Documentos Relacionados
- Cloning and DNA sequence of the omc gene encoding the outer membrane protein-macromolecular complex from Neisseria gonorrhoeae.
- One-dimensional peptide mapping of the major outer membrane protein of Neisseria gonorrhoeae.
- High-molecular-weight antigenic protein complex in the outer membrane of Neisseria gonorrhoeae.
- Identification and purification of a hemoglobin-binding outer membrane protein from Neisseria gonorrhoeae.
- Altered outer membrane protein in different colonial types of Neisseria gonorrhoeae.
