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Identifying the major proteome components of Helicobacter pylori strain 26695
Author(s) -
Cho MyungJe,
Jeon BeongSam,
Park JeongWon,
Jung TaeSung,
Song JaeYoung,
Lee WooKon,
Choi YeoJeong,
Choi SangHaeng,
Park SeongGyu,
Park JeongUck,
Choe MiYoung,
Jung SeunAe,
Byun EunYoung,
Baik SeungChul,
Youn HeeShang,
Ko GyungHyuck,
Lim DongBin,
Rhee KwangHo
Publication year - 2002
Publication title -
electrophoresis
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.666
H-Index - 158
eISSN - 1522-2683
pISSN - 0173-0835
DOI - 10.1002/1522-2683(200204)23:7/8<1161::aid-elps1161>3.0.co;2-7
Subject(s) - proteome , strain (injury) , helicobacter pylori , protein subunit , gel electrophoresis , ammonium sulfate , biochemistry , two dimensional gel electrophoresis , spots , biology , chemistry , gene , electrophoresis , saturation (graph theory) , ammonium , microbiology and biotechnology , chromatography , proteomics , genetics , botany , mathematics , organic chemistry , anatomy , combinatorics
The whole genome sequences of Helicobacter pylori strain 26695 have been reported. Whole cell proteins of H. pylori strain 26695 cells were obtained and analyzed by two‐dimensional electrophoresis, using immobilized pH gradient strips. The most abundant proteins were shown in the region of p I 4.0–9.5 with molecular masses from 10 to 100 kDa. Soluble proteins were precipitated by the use of 0–80% saturated solutions of ammonium sulfate. Soluble proteins precipitated by the 0–40% saturations of ammonium sulfate produced similar spot profiles and their abundant protein spots had acidic p I regions. However, a number of soluble proteins precipitated by more than 60% saturation of ammonium sulfate were placed in the alkaline p I regions, compared to those precipitated by 40% saturation. In addition, we have performed an extensive proteome analysis of the strain utilizing peptide MALDI‐TOF‐MS. Among the 345 protein spots processed, 175 proteins were identified. The identified spots represented 137 genes. One‐hundred and fifteen proteins were newly identified in this study, including DNA polymerase III β‐subunit. These results might provide guidance for the enrichment of H. pylori proteins and contribute to construct a master protein map of H. pylori .