Application of Hemin-Agarose Affinity Chromatography to Enrich Proteome Components of Helicobacter pylori Strain 26695
Journal of Bacteriology and Virology
; : 77-85, 2005.
Article
en En
| WPRIM
| ID: wpr-9660
Biblioteca responsable:
WPRO
ABSTRACT
The whole cell extract of Helicobacter pylori strain 26695 was treated with the hemin-agarose resin and the bound fraction was analyzed by 2-Dimensional electrophoresis. The 2-D-PAGE-displayed spots were eluted and analyzed by matrix-assisted laser desorption ionization mass spectrometry (MALDI-MS). Among the 120 spots processed, 94 protein spots were identified to represent 58 genes. Forty-five protein spots that represented thirty-four genes were newly identified in this study, including iron-containing proteins and hemin-containg proteins such as fumarate reductase, iron-sufur subunit(FrdB), ribonucleoside diphosphate reductase, beta subunit (NrdB), glutamyl-tRNA reductase (HemA), nikel-cobalt-cadnium resistance protein (NccB), and porphobilinogen deaminase (HemC).
Palabras clave
Texto completo:
1
Índice:
WPRIM
Asunto principal:
Oxidorreductasas
/
Hidroximetilbilano Sintasa
/
Ribonucleósido Difosfato Reductasa
/
Espectrometría de Masas
/
Succinato Deshidrogenasa
/
Cromatografía de Afinidad
/
Helicobacter pylori
/
Helicobacter
/
Proteoma
/
Electroforesis
Idioma:
En
Revista:
Journal of Bacteriology and Virology
Año:
2005
Tipo del documento:
Article