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Application of Hemin-Agarose Affinity Chromatography to Enrich Proteome Components of Helicobacter pylori Strain 26695
Journal of Bacteriology and Virology ; : 77-85, 2005.
Article in English | WPRIM | ID: wpr-9660
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).
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Full text: Available Index: WPRIM (Western Pacific) Main subject: Oxidoreductases / Hydroxymethylbilane Synthase / Ribonucleoside Diphosphate Reductase / Mass Spectrometry / Succinate Dehydrogenase / Chromatography, Affinity / Helicobacter pylori / Helicobacter / Proteome / Electrophoresis Language: English Journal: Journal of Bacteriology and Virology Year: 2005 Type: Article

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Full text: Available Index: WPRIM (Western Pacific) Main subject: Oxidoreductases / Hydroxymethylbilane Synthase / Ribonucleoside Diphosphate Reductase / Mass Spectrometry / Succinate Dehydrogenase / Chromatography, Affinity / Helicobacter pylori / Helicobacter / Proteome / Electrophoresis Language: English Journal: Journal of Bacteriology and Virology Year: 2005 Type: Article