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

Per Hägglund, Jakob Bunkenborg, Fen Yang, Lea Mørch Harder, Christine Finnie, Birte Svensson

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Abstrakt

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.
OriginalsprogEngelsk
TidsskriftJournal of Proteomics
Vol/bind73
Udgave nummer6
Sider (fra-til)1133-6
Antal sider4
ISSN1874-3919
DOI
StatusUdgivet - 18. apr. 2010

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