Conservation of peptide structure of outer membrane protein-macromolecular complex from Neisseria gonorrhoeae
| Autor: | C E Wilde, M V Hansen |
|---|---|
| Rok vydání: | 1984 |
| Předmět: |
Macromolecular Substances
Sequence analysis Immunology Peptide Biology Microbiology chemistry.chemical_compound Amino Acid Sequence Peptide sequence Chromatography High Pressure Liquid Dansyl Compounds chemistry.chemical_classification Dansyl chloride Protein primary structure Membrane Proteins Neisseria gonorrhoeae Amino acid Infectious Diseases Isoelectric point chemistry Biochemistry Parasitology Isoelectric Focusing Peptides Bacterial outer membrane Research Article Bacterial Outer Membrane Proteins |
| Zdroj: | Infection and Immunity. 43:839-845 |
| ISSN: | 1098-5522 0019-9567 |
| DOI: | 10.1128/iai.43.3.839-845.1984 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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