J Korean Acad Periodontol.  2002 Jun;32(2):351-360. 10.5051/jkape.2002.32.2.351.

Isolation and Partial Characterization of a 50 kDa Hemin-regulated Cell Envelope Protein from Prevotella nigrescens

• Kim KM
• Choi JI
• Kim SJ

• KMID: 2057046
• DOI: http://doi.org/10.5051/jkape.2002.32.2.351

Abstract

In the study presented here, identification, purification, and partial characterization of a hemin-regulated protein in Prevotella nigrescens were carried out. The results of this study confirm that the availability of hemin influences the expression of a selected membrane protein as well as the growth rate of P. nigrescens ATCC 33563. The 50 kDa cell envelope associated protein, whose expression is hemin regulated, is considered to be a putative hemin-binding protein from P. nigrescens. Disulfide bonds were not present in this protein, and N'-terminal amino acid sequence analysis revealed that this protein belongs to a new, so far undescribed protein. The 50 kDa protein was found to be rich in hydrophilic amino acids, with glycine comprising approximately 60% of the total amino acids. The study described here is the first to identify, purify, and biochemically characterize a putative hemin-binding protein from P. nigrescens. Work is in progress to further characterize the molecular structure of this protein.

Keyword

Hemin; Cell envelope protein; Prevotella nigrescens

MeSH Terms

Amino Acids
Glycine
Hemin
Membrane Proteins
Molecular Structure
Prevotella nigrescens*
Prevotella*
Sequence Analysis, Protein
Amino Acids
Glycine
Hemin
Membrane Proteins