J Bacteriol Virol.  2005 Jun;35(2):77-85.

Application of Hemin-Agarose Affinity Chromatography to Enrich Proteome Components of Helicobacter pylori Strain 26695

Affiliations
  • 1Department of Microbiology, Gyeongsang National University College of Medicine, Korea. scbaik@gaechuk.gsnu.ac.kr
  • 2Gyeongsang Institute of Health Science, 90 Chiram-dong, Jinju, Gyeongsangnam-do 660-751, Korea.
  • 3Research Institute of Life Science and Central Laboratory, Gyeongsang National University, 900 Gajwa-dong, Jinju, Gyeongsangnam-do 660-751, Korea.

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).

Keyword

Hemin-agarose chromatography; Helicobacter pylori; Matrix-assisted laser desorption ionization mass spectroscopy; Proteome; Two-dimensional electrophoresis

MeSH Terms

Chromatography, Affinity*
Electrophoresis
Helicobacter pylori*
Helicobacter*
Hydroxymethylbilane Synthase
Mass Spectrometry
Oxidoreductases
Proteome*
Ribonucleoside Diphosphate Reductase
Succinate Dehydrogenase
Hydroxymethylbilane Synthase
Oxidoreductases
Proteome
Ribonucleoside Diphosphate Reductase
Succinate Dehydrogenase
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