Determination of in vivo disulfide-bonded proteins in Arabidopsis

被引：14

作者：

Alvarez, Sophie ^{[1
]}

Wilson, Gordon H. ^{[1
]}

Chen, Sixue ^{[1
,2
]}

机构：

[1] Univ Florida, Dept Bot & Zool, Gainesville, FL 32610 USA

[2] Univ Florida, Interdisciplinary Ctr Biotechnol Res, Proteom Facil, Gainesville, FL 32610 USA

来源：

JOURNAL OF CHROMATOGRAPHY B-ANALYTICAL TECHNOLOGIES IN THE BIOMEDICAL AND LIFE SCIENCES | 2009年 / 877卷 / 1-2期

基金：

美国国家科学基金会;

关键词：

Arabidopsis; Disulfide bonds; Thiol labeling; Proteomics; Mass spectrometry; REDOX REGULATION; IDENTIFICATION; THIOREDOXIN; ISOMERASE; PROTEOME; PLANTS;

D O I：

10.1016/j.jchromb.2008.11.027

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

Protein thiol-disulfide oxidoreduction plays an important role in redox regulation of cellular processes. Here we present a proteomic approach to visualize and map in vivo disulfide-bonded proteins in plants. A proteomic map of the disulfide-bonded proteins was achieved using 2D gel electrophoresis of Arabidopsis protein extract. Along with novel proteins identified as potentially redox regulated, we have also shown the feasibility of mapping some of the cysteines involved in the formation of disulfide bonds. This study presents an important tool for characterizing redox-regulated proteins. (C) 2008 Elsevier B.V. All rights reserved.

引用

页码：101 / 104

页数：4

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