Determination of in vivo disulfide-bonded proteins in Arabidopsis

Sophie Alvarez, Gordon H. Wilson, Sixue Chen

Research output: Contribution to journalArticle

13 Citations (Scopus)

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.

Original languageEnglish (US)
Pages (from-to)101-104
Number of pages4
JournalJournal of Chromatography B: Analytical Technologies in the Biomedical and Life Sciences
Volume877
Issue number1-2
DOIs
StatePublished - Jan 1 2009

Fingerprint

Arabidopsis Proteins
Disulfides
Oxidation-Reduction
Proteomics
Proteins
Plant Proteins
Electrophoresis, Gel, Two-Dimensional
Sulfhydryl Compounds
Cysteine
Electrophoresis
Gels

Keywords

  • Arabidopsis
  • Disulfide bonds
  • Mass spectrometry
  • Proteomics
  • Thiol labeling

ASJC Scopus subject areas

  • Analytical Chemistry
  • Biochemistry
  • Clinical Biochemistry
  • Cell Biology

Cite this

Determination of in vivo disulfide-bonded proteins in Arabidopsis. / Alvarez, Sophie; Wilson, Gordon H.; Chen, Sixue.

In: Journal of Chromatography B: Analytical Technologies in the Biomedical and Life Sciences, Vol. 877, No. 1-2, 01.01.2009, p. 101-104.

Research output: Contribution to journalArticle

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