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PMID: 8827708 Published · ppublish English Journal Article Research Support, U.S. Gov't, P.H.S.

Isolation and characterization of a hemin-binding cell envelope protein from Porphyromonas gingivalis.

Microbial pathogenesis ·Vol. 21 ·No. 1 ·1996-07-00 ·Pages 65-70

Kim SJ, Chu L, Holt SC

Abstract

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.

MeSH Terms
Amino Acid Sequence Bacterial Outer Membrane Proteins/chemistry,isolation & purification,metabolism Benzaldehydes/metabolism Cyanogen Bromide/metabolism Electrophoresis, Polyacrylamide Gel Hemin/metabolism Iron/metabolism Molecular Sequence Data Porphyromonas gingivalis/chemistry,growth & development Protein Binding Staining and Labeling
Chemicals
Bacterial Outer Membrane Proteins Benzaldehydes 2,4,5-trimethoxybenzaldehyde Hemin Iron Cyanogen Bromide
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Kim S J
Department of Microbiology, University of Texas Health Center at San Antonio 78284, USA.
Chu L
Holt S C
Article Info
Journal
Microbial pathogenesis
Abbr.
Microb Pathog
ISSN
0882-4010
Published
1996-07-00
Pages
65-70
Language
English
Region
England
NLM ID
8606191
Subset
IM
Grants
NIDCR NIH HHS · DE-07627 · United States
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