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    National Tsing Hua University Institutional Repository > 生命科學院  > 生命科學系 > 期刊論文 >  One-Step Chromatographic Purification of Helicobacter pylori Neutrophil-Activating Protein Expressed in Bacillus subtilis


    Please use this identifier to cite or link to this item: http://nthur.lib.nthu.edu.tw/dspace/handle/987654321/81432


    Title: One-Step Chromatographic Purification of Helicobacter pylori Neutrophil-Activating Protein Expressed in Bacillus subtilis
    Authors: Kuo-Shun Shih;Chih-Chang Lin;Hsiao-Fang Hung;Yu-Chi Yang;Chung-An Wang;Kee-Ching Jeng;Hua-Wen Fu
    教師: 傅化文
    Date: 2013
    Publisher: Public Library of Science
    Relation: PLoS One, Public Library of Science, Volume 8, Issue 4, APR 2013, e60786
    Keywords: ION-EXCHANGE CHROMATOGRAPHY
    HP-NAP
    INFLAMMATION
    IMMUNOGENICITY
    EPIDEMIOLOGY
    ANTIBODIES
    RETENTION
    RESPONSES
    ANTIGEN
    SAFETY
    Abstract: Helicobacter pylori neutrophil-activating protein (HP-NAP), a major virulence factor of Helicobacter pylori (H. pylori), is capable of activating human neutrophils to produce reactive oxygen species (ROS) and secrete inammatory mediators. HP-NAP is a vaccine candidate, a possible drug target, and a potential in vitro diagnostic marker for H. pylori infection. HP-NAP has also been shown to be a novel therapeutic agent for the treatment of allergic asthma and bladder cancer. Hence, an efficient way to obtain pure HP-NAP needs to be developed. In this study, one-step anion-exchange chromatography in negative mode was applied to purify the recombinant HP-NAP expressed in Bacillus subtilis (B. subtilis). This purification technique was based on the binding of host cell proteins and/or impurities other than HP-NAP to DEAE Sephadex resins. At pH 8.0, almost no other proteins except HP-NAP passed through the DEAE Sephadex column. More than 60% of the total HP-NAP with purity higher than 91% was recovered in the flow-through fraction from this single-step DEAE Sephadex chromatography. The purified recombinant HP-NAP was further demonstrated to be a multimeric protein with a secondary structure of α-helix and capable of activating human neutrophils to stimulate ROS production. Thus, this one-step negative chromatography using DEAE Sephadex resin can efficiently yield functional HP-NAP from B. subtilis in its native form with high purity. HP-NAP purified by this method could be further utilized for the development of new drugs, vaccines, and diagnostics for H. pylori infection.
    Relation Link: http://www.plos.org/
    URI: http://nthur.lib.nthu.edu.tw/dspace/handle/987654321/81432
    Appears in Collections:[生命科學系] 期刊論文
    [分子與細胞生物研究所] 期刊論文

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