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KMID : 0921620070370040203
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Journal of Bacteriology and Virology
2007 Volume.37 No. 4 p.203 ~ p.212
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Proteomic Analysis of Helicobacter pylori Whole Cell Proteins using the Narrow Range IPG Strips
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Park Jeong-Won
Seo Ji-Hyun
Kang Hyung-Lyun
Song Jae-Young
Cho Myung-Je
Jun Jin-Su
Youn Hee-Shang
Lee Seung-Gyu
Joo Jung-Soo
Baik Seung-Chul
Lee Woo-Kon
Rhee Kwang-Ho
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Abstract
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It has been reported that most of Helicobacter pylori proteome components appear so crowded in the region of pH 4.5~8.0 that a lot of them were inseparable in 2-DE using the broad range IPG strip. Therefore, inseparable protein spots in 2-DE profiles have to be apart from each other for improving the protein identification. Here, we attempt to examine the usability of the narrow range IPG strips for separating close spots in the broad range IPG strip at proteomic analysis of H. pylori. The whole cell proteins of H. pylori strain 26695 were separated by narrow range IPG strips (pI 3.9~5.1, 4.7~5.9, 5.5~6.7, and 6.3~8.3, respectively), followed by SDS-PAGE, and visualized by silver staining, showing that the distances between spots were widened and the total number of detectable spots was increased. Resolved protein spots were identified by the peptide fingerprinting using MALDI-TOF-MS. As a result, 87 expressed proteins were identified by the peptide fingerprinting. Of them, 23 proteins, including hydrogenase expression/formation protein, purine-binding chemotaxis protein, and ribosomal protein S6, have not been reported in the previous proteome studies of H. pylori. Thus, these results demonstrate that the high complexity proteome components could be effectively separated using the narrow range IPG strips, which might be helpful to strengthen the contents of the master protein map of the H. pylori reference strain.
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KEYWORD
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Narrow range IPG strip, Helicobacter pylori, Proteomics
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