Meiho University Institutional Repository:Item 987654321/1230
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    题名: Identification of low-abundance proteins via fractionation of the urine proteome with weak anion exchange chromatography
    作者: Chih-Ming Lu;Yu-Jen Wu;Cheng-Chi Chen;Jue-Liang Hsu;Jiing-Chuan Chen;Jeff Yi-Fu Chen;Chun-Hsiung Huang;Ying-Chin Ko
    关键词: Weak anion exchange chromatography DEAE-Sephacel;Fractionation;Proteomic;Urine
    日期: 2011-04
    上传时间: 2011-09-28T03:58:03Z (UTC)
    摘要: Background: Low-abundance proteins are difficultly observed on the two-dimensional gel electrophoresis (2-DE)
    maps of urine proteome, because they are usually obscured by high-abundance proteins such as albumin and
    immunoglobulin. In this study, a novel fractionation method was developed for enriching low-abundance proteins
    by removing high-abundance proteins and progressive elution with salts of various concentrations.
    Results: Stepwise weak anion exchange (WAX) chromatography, which applied DEAE-Sephacel resin with nonfixed
    volume elution, was used to fractionate urine proteome prior to performing 2-DE. Urine proteome was
    separated into four fractions by progressively eluting the column with 0 M, 50 mM, 100 mM, and 1 M NaCl
    solutions. Most of the heavy and light immunoglobulin chains appeared in the eluent. After the high-abundance
    proteins were removed, various low-abundance proteins were enriched and could be easily identified. The
    potential of this method for obtaining diversified fractionations was demonstrated by eluting the column
    separately with Na2SO4 and MgCl2 solutions. The 2-DE maps of the fractions eluted with these different salt
    solutions of identical ionic strength revealed markedly different stain patterns.
    Conclusion: The present study demonstrated that this fractionation method could be applied for purposes of
    enriching low-abundance proteins and obtaining diversified fractionations of urine, and potentially other
    proteomes.
    關聯: Proteome Sci. 2011 Apr 8;9:17
    显示于类别:[美容系] 期刊論文

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