Isolation and Partial Characterization of Hemin-binding Cell Envelope Proteins from Porphyromonas gingivalis, Prevotella intermedia, and Prevotella nigrescens / 대한치주과학회지
The Journal of the Korean Academy of Periodontology
;
: 155-165, 2006.
Article
in Korean
| WPRIM
| ID: wpr-10073
ABSTRACT
The results of this study confirm that the availability of hemin influences the expression of selected membrane proteins of Porphyromonas gingivalis, Prevotella intermedia, and Prevotella nigrescens. A 30 kDa (heated 24 kDa) hemin-binding protein whose expression is hemin regulated was identified and purified in P. gingivalis. A strong hemin-binding function was found by LDS-PAGE and TMBZ staining when P. gingivalis cells were grown under hemin-limited conditions. A 50 kDa cell envelope associated protein, whose expression is hemin regulated, is considered to be a putative hemin binding protein from P. intermedia and P. nigrescens, respectively. N-terminal amino acid sequence analysis of CNBr-digested 24 kDa hemin binding protein from P. gingivalis revealed that this protein belongs to a new, so far undescribed hemin-binding class of proteins. N-terminal amino acid sequence of a 50 kDa putative hemin binding protein from P. intermedia was identical with Enolase from Streptococcus intermedia. Work is in progress to further characterize the molecular structure of these proteins.
Full text:
Available
Index:
WPRIM (Western Pacific)
Main subject:
Phosphopyruvate Hydratase
/
Streptococcus
/
Molecular Structure
/
Carrier Proteins
/
Amino Acid Sequence
/
Porphyromonas
/
Porphyromonas gingivalis
/
Prevotella intermedia
/
Prevotella
/
Sequence Analysis, Protein
Language:
Korean
Journal:
The Journal of the Korean Academy of Periodontology
Year:
2006
Type:
Article
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