Abstract
A 30 kDa (heated 24 kDa) hemin-binding protein whose expression is both hemin and iron regulated was identified and purified in Porphyromonas gingivalis 381. A strong hemin-binding function was found by LDS-PAGE and TMBZ staining when cells were grown under hemin (iron)-limited conditions. N-terminal amino acid sequence analysis of CNBr-digested 24 kDa hemin binding protein revealed that this protein belongs to a new, so far undescribed hemin-binding class of proteins.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 65-70 |
| Number of pages | 6 |
| Journal | Microbial Pathogenesis |
| Volume | 21 |
| Issue number | 1 |
| DOIs | |
| State | Published - Jul 1996 |
Keywords
- Hemin
- Outer membranes
- Porphyromonas gingivalis
- TMBZ
ASJC Scopus subject areas
- Microbiology
- Infectious Diseases
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Cite this
Kim, S. J., Chu, L., & Holt, S. C. (1996). Isolation and characterization of a hemin-binding cell envelope protein from Porphyromonas gingivalis. Microbial Pathogenesis, 21(1), 65-70. https://doi.org/10.1006/mpat.1996.0043