Application of Hemin-Agarose Affinity Chromatography to Enrich Proteome Components of Helicobacter pylori Strain 26695.
- Author:
Hyung Lyun KANG
1
;
Seung Chul BAIK
Author Information
1. Department of Microbiology, Gyeongsang National University College of Medicine, Korea. scbaik@gaechuk.gsnu.ac.kr
- Publication Type:Original Article
- Keywords:
Hemin-agarose chromatography;
Helicobacter pylori;
Matrix-assisted laser desorption ionization mass spectroscopy;
Proteome;
Two-dimensional electrophoresis
- MeSH:
Chromatography, Affinity*;
Electrophoresis;
Helicobacter pylori*;
Helicobacter*;
Hydroxymethylbilane Synthase;
Mass Spectrometry;
Oxidoreductases;
Proteome*;
Ribonucleoside Diphosphate Reductase;
Succinate Dehydrogenase
- From:Journal of Bacteriology and Virology
2005;35(2):77-85
- CountryRepublic of Korea
- Language:English
-
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).
