Isolation and Partial Characterization of a 50 kDa Hemin-regulated Cell Envelope Protein from Prevotella nigrescens.
10.5051/jkape.2002.32.2.351
- Author:
Kyung Mi KIM
1
;
Jeom IL CHOI
;
Sung Jo KIM
Author Information
1. Department of Periodontology, College of Dentistry, Pusan National University, Korea.
- Publication Type:Original Article
- Keywords:
Hemin;
Cell envelope protein;
Prevotella nigrescens
- MeSH:
Amino Acids;
Glycine;
Hemin;
Membrane Proteins;
Molecular Structure;
Prevotella nigrescens*;
Prevotella*;
Sequence Analysis, Protein
- From:The Journal of the Korean Academy of Periodontology
2002;32(2):351-360
- CountryRepublic of Korea
- Language:Korean
-
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.
