Analysis of Low Molecular Weight Proteome from H. pylori Cell Extract Using the High Performance Liquid Chromatography.
- Author:
Jung Won PARK
1
;
Kyung Ja LEE
;
Kyung Mi KIM
;
Jung Soo JOO
;
Yung Chul KWON
;
Hee Shang YOUN
;
Jae Young SONG
;
Hyung Lyun KANG
;
Kon Ho LEE
;
Seung Chul BAIK
;
Woo Kon LEE
;
Myung Je CHO
;
Kwang Ho RHEE
Author Information
- Publication Type:Original Article
- Keywords: Helicobacter pylori; Hybrid tandem mass spectrometer; Low molecular protein
- MeSH: Acrylic Resins; Carrier Proteins; Catalase; Chimera; Chromatography, High Pressure Liquid; Chromatography, Liquid; Copper; Electrophoresis; Electrophoresis, Polyacrylamide Gel; Helicobacter pylori; Molecular Weight; Pepsin A; Peptides; Proteins; Proteome; Ribosomal Proteins; Thioredoxins
- From:Journal of Bacteriology and Virology 2010;40(2):67-75
- CountryRepublic of Korea
- Language:Korean
- Abstract: Low molecular proteins (LMPs) which are smaller than 20 kDa are difficult to visible on a standard two-dimensional SDS-polyacrylamide gel electrophoresis (2-D SDS-PAGE) map. LMPs must be enriched appropriately to be analyzed. We isolated LMPs of Helicobacter pylori 26695 from 1-D polyacrylamide gel and digested by pepsin. Pepsin-digested LMPs were separated by HPLC and each fraction was analyzed by hybrid tandem mass spectrometer. Seventy nine peptides, representing 27 genes, including copper ion binding protein (CopP, 7 kDa), thioredoxin (TrxA, 11.9 kDa) and ribosomal protein L23 (Rpl23, 10.5 kDa) were identified. Some proteins larger than 40 kDa including Omp2, Omp21, Omp27, Omp30, Omp32, catalase and HP1083 were also identified. This work may give researchers a useful way to analyse the expressed LMPs which could not be identified on the conventional 2-D SDS-PAGE.
