Isolation and Partial Characterization of Hemin-binding Cell Envelope Proteins from Porphyromonas gingivalis, Prevotella intermedia, and Prevotella nigrescens.
10.5051/jkape.2006.36.1.155
- Author:
Sung Jo KIM
1
Author Information
1. Department of Periodontology, School of Dentistry, Pusan National University, Korea.
- Publication Type:Original Article
- Keywords:
Hemin;
Cell envelope proteins;
Porphyromonas gingivalis;
Prevotella intermedia;
Prevotella nigrescens
- MeSH:
Amino Acid Sequence;
Carrier Proteins;
Hemin;
Membrane Proteins;
Molecular Structure;
Phosphopyruvate Hydratase;
Porphyromonas gingivalis*;
Porphyromonas*;
Prevotella intermedia*;
Prevotella nigrescens*;
Prevotella*;
Sequence Analysis, Protein;
Streptococcus
- From:The Journal of the Korean Academy of Periodontology
2006;36(1):155-165
- CountryRepublic of Korea
- Language:Korean
-
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.
