J Korean Acad Periodontol.  2006 Mar;36(1):155-165.

Isolation and Partial Characterization of Hemin-binding Cell Envelope Proteins from Porphyromonas gingivalis, Prevotella intermedia, and Prevotella nigrescens

• Kim SJ

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.

Keyword

Hemin; Cell envelope proteins; Porphyromonas gingivalis; Prevotella intermedia; Prevotella nigrescens

MeSH Terms

Amino Acid Sequence
Carrier Proteins
Hemin
Membrane Proteins
Molecular Structure
Phosphopyruvate Hydratase
Porphyromonas gingivalis*
Porphyromonas*
Prevotella intermedia*
Prevotella nigrescens*
Prevotella*
Sequence Analysis, Protein
Streptococcus
Carrier Proteins
Hemin
Membrane Proteins
Phosphopyruvate Hydratase