| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 1216457 | Journal of Chromatography B | 2009 | 4 Pages |
Abstract
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.
Related Topics
Physical Sciences and Engineering
Chemistry
Analytical Chemistry
Authors
Sophie Alvarez, Gordon H. Wilson, Sixue Chen,