Expression of the C-terminal 26 kDa fragment of Helicobacter pylori UreB in Escherichia coli and its immunity

A 720 bp fragment of ureB encoding the urease beta subunits of Helicobacter pylori was cloned into an expression vector (pAMJ399) and expressed in Escherichia coli JM109 cells. The recombinant rUreB-E fractions of UreB displayed molecular masses of approximate 26 kDa estimated by SDS-PAGE. Western b...

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Bibliographic Details
Main Authors: GU Qing, YAO Lei, LI Jian-rong, ZHU Mu-yuan
Format: Article
Language:English
Published: Zhejiang University Press 2006-07-01
Series:浙江大学学报. 农业与生命科学版
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Online Access:https://www.academax.com/doi/10.3785/1008-9209.2006.04.0387
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Summary:A 720 bp fragment of ureB encoding the urease beta subunits of Helicobacter pylori was cloned into an expression vector (pAMJ399) and expressed in Escherichia coli JM109 cells. The recombinant rUreB-E fractions of UreB displayed molecular masses of approximate 26 kDa estimated by SDS-PAGE. Western blotting analysis indicated that the proteins were strongly immunogenic and were specifically recognized by polyclonal human anti-Helicobacter pylori sera. ELISA tests showed serum from Balb/c mice immunized with the recombinant protein was able to induce anti-UreB serum antibody, and that the protein qualified immunoreactivity and antigenicity.
ISSN:1008-9209
2097-5155