Abstract
A major cell envelope protein was purified from the cell envelope fraction of Treponema denticola ATCC 35405 by ion exchange chromatography after extraction with Zwittergent 3–14. Sodium dodecyl sulfate‐polyacrylamide gel electro‐phoresis showed a relative molecular mass of 53 kDa for this protein with a pI of 6.3–6.8. Amino acid analysis revealed that this protein contained high proportions of hydrophobic amino acids (40.4%), and no cysteine could be detected. The N‐terminus of the protein was blocked to Edman degradation. Rabbit antiserum raised against the purified 53 kDa protein reacted with the outer envelope of the T. denticola cell surface as confirmed by immunoelectron microscopy. This rabbit antiserum reacted with 4 of the 11 strains of treponemes tested in this study. Sera from 9 to 18 periodontitis patients reacted strongly with this 53 kDa cell envelope protein of T. denticola as determined by immunoblotting analysis.
| Original language | English |
|---|---|
| Pages (from-to) | 70-78 |
| Number of pages | 9 |
| Journal | Journal of Periodontal Research |
| Volume | 29 |
| Issue number | 1 |
| DOIs | |
| Publication status | Published - Jan 1994 |
Keywords
- Treponema denticola
- immunoreactivity
- isolation and characterization
- major cell envelope protein
ASJC Scopus subject areas
- Periodontics