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鉴定从小麦糊粉层中释放的蛋白质中的硫氧还蛋白靶二硫键。

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

机构信息

Enzyme and Protein Chemistry, Department of Systems Biology, Søltofts Plads, Building 224, Technical University of Denmark, DK-2800 Kgs. Lyngby, Denmark.

出版信息

J Proteomics. 2010 Apr 18;73(6):1133-6. doi: 10.1016/j.jprot.2010.01.007. Epub 2010 Jan 28.

DOI:10.1016/j.jprot.2010.01.007
PMID:20114090
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.

摘要

硫氧还蛋白是一种普遍存在的二硫键还原酶,参与多种细胞过程,包括 DNA 合成、氧化应激反应和细胞凋亡。在谷类种子中,硫氧还蛋白被认为通过还原贮藏蛋白和淀粉胚乳中其他靶标中的二硫键来促进萌发过程。在这里,我们应用巯基特异性标记方法来鉴定在含有赤霉素的缓冲液中培养的大麦糊粉层释放的蛋白质中大麦硫氧还蛋白的特定二硫键靶标。

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