Isolation and characterization of a hemin-binding cell envelope protein from Porphyromonas gingivalis.
A 30 kDa (heated 24 kDa) hemin-binding protein whose expression is both hemin and iron regulated was identified and purified in Porphyromonas gingivalis 381. A strong hemin-binding function was found by LDS-PAGE and TMBZ staining when cells were grown under hemin (iron)-limited conditions. N-terminal amino acid sequence analysis of CNBr-digested 24 kDa hemin binding protein revealed that this protein belongs to a new, so far undescribed hemin-binding class of proteins.
Kim
S J
SJ
Department of Microbiology, University of Texas Health Center at San Antonio 78284, USA.
Chu
L
L
Holt
S C
SC
D000595:Amino Acid Sequence; D001425:Bacterial Outer Membrane Proteins / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism*; D001547:Benzaldehydes / Q000378:metabolism; D003488:Cyanogen Bromide / Q000378:metabolism; D004591:Electrophoresis, Polyacrylamide Gel; D006427:Hemin / Q000378:metabolism*; D007501:Iron / Q000378:metabolism; D008969:Molecular Sequence Data; D016966:Porphyromonas gingivalis / Q000737:chemistry* / Q000254:growth & development; D011485:Protein Binding; D013194:Staining and Labeling
D001425:Bacterial Outer Membrane Proteins; D001547:Benzaldehydes; C034031:2,4,5-trimethoxybenzaldehyde; D006427:Hemin; D007501:Iron; D003488:Cyanogen Bromide