Identification of thioredoxin target disulfides in proteins released from barley aleurone layers

Per Hägglund, J. Bunkenborg, Fen Yang, L.M. Harder, Christine Finnie, Birte Svensson

    Research output: Contribution to journalJournal articleResearchpeer-review

    Abstract

    Thioredoxins are ubiquitous disulfide reductases involved in a wide range of cellular processes including DNA synthesis, oxidative stress response and apoptosis. In cereal seeds thioredoxins are proposed to facilitate the germination process by reducing disulfide bonds in storage proteins and other targets in the starchy endosperm. Here we have applied a thiol-specific labeling approach to identify specific disulfide targets of barley thioredoxin in proteins released from barley aleurone layers incubated in buffer containing gibberellic acid.
    Original languageEnglish
    JournalJournal of Proteomics
    Volume73
    Issue number6
    Pages (from-to)1133-1136
    ISSN1874-3919
    DOIs
    Publication statusPublished - 2010

    Keywords

    • Thioredoxin
    • Redox proteomics
    • Isotope-coded affinity tag
    • Disulfide
    • Aleurone layer
    • Barley germination

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