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

Publication: Research - peer-reviewJournal article – Annual report year: 2010

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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
Publication date2010
Volume73
Issue6
Pages1133-1136
ISSN1874-3919
DOIs
StatePublished
CitationsWeb of Science® Times Cited: 11

Keywords

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