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

Research output: Contribution to journalJournal articleResearchpeer-review

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
Issue number6
Pages (from-to)1133-1136
Number of pages4
Publication statusPublished - 2010
Externally publishedYes

    Research areas

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

ID: 240160404