Abstract
The major outer membrane proteins (MOMP) of 53 and 67 kDa were identified by sodium dodecyl sulphate-polyacrylamide gel electrophoresis in outer membrane enriched fractions of Porphyromonas gingivalis FDC 381 and ATCC 33277, respectively. The MOMP were purified by anion exchange and gel filtration chromatography after extraction with Zwittergent 3-14. Their reactivity to monoclonal antibodies and their amino acid composition were analysed. The N-terminal amino acid sequences of twenty residues of both purified MOMP were determined and compared with those previously reported for MOMP of other periodontopathic bacteria.
| Original language | English |
|---|---|
| Pages (from-to) | 247-252 |
| Number of pages | 6 |
| Journal | Microbios |
| Volume | 77 |
| Issue number | 313 |
| Publication status | Published - 1994 |
ASJC Scopus subject areas
- Microbiology
- Microbiology (medical)