Proteomic Analysis of Thiol-active Proteins of Helicobacter pylori 26695
Journal of Bacteriology and Virology
;
: 211-223, 2012.
Artigo
em Inglês
| WPRIM
| ID: wpr-170984
ABSTRACT
Helicobacter pylori are a capnophilic bacterium, which colonize gastric mucosa and are resistant to acidic and oxidative damage. Thiol-active proteins subserve redox functions in tolerating oxidative stress and environmental toxicants, such as hydrogen peroxide and hypochlorous acid. We analyzed disulfide-containing proteins of H. pylori strain 26695. Active disulfide-containing proteins were separated by thiol-affinity chromatography, displayed with two-dimensional electrophoresis (2-DE), and identified by MALDI-TOF-MS. Thirty-five putative disulfide proteins, including AhpC (HP1563), GroEL (HP0011), and FrdB (HP0191), were identified in this study. In addition, 4 disulfide proteins of HypB, FusA, TufB, and AhpC showed enhanced intensities in the periplasmic space when compared with the pellet, suggesting that these proteins might play roles in the first redox system against environmental oxidative stresses. Disulfide-containing proteins identified in this study will provide the standard landscape for constructing the proteome components responsible for redox regulation of H. pylori.
Texto completo:
DisponíveL
Índice:
WPRIM (Pacífico Ocidental)
Assunto principal:
Oxirredução
/
Entorses e Distensões
/
Proteínas
/
Cromatografia
/
Helicobacter pylori
/
Helicobacter
/
Colo
/
Ácido Hipocloroso
/
Estresse Oxidativo
/
Periplasma
Idioma:
Inglês
Revista:
Journal of Bacteriology and Virology
Ano de publicação:
2012
Tipo de documento:
Artigo
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