Determination of in vivo disulfide-bonded proteins in Arabidopsis

Sophie Alvarez; Gordon H. Wilson; Sixue Chen

doi:10.1016/j.jchromb.2008.11.027

Determination of in vivo disulfide-bonded proteins in Arabidopsis

Sophie Alvarez, Gordon H. Wilson, Sixue Chen

Research output: Contribution to journal › Article › peer-review

14 Scopus citations

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 language	English (US)
Pages (from-to)	101-104
Number of pages	4
Journal	Journal of Chromatography B: Analytical Technologies in the Biomedical and Life Sciences
Volume	877
Issue number	1-2
DOIs	https://doi.org/10.1016/j.jchromb.2008.11.027
State	Published - Jan 1 2009
Externally published	Yes

Keywords

Arabidopsis
Disulfide bonds
Mass spectrometry
Proteomics
Thiol labeling

ASJC Scopus subject areas

Analytical Chemistry
Biochemistry
Clinical Biochemistry
Cell Biology

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10.1016/j.jchromb.2008.11.027

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title = "Determination of in vivo disulfide-bonded proteins in Arabidopsis",

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.",

keywords = "Arabidopsis, Disulfide bonds, Mass spectrometry, Proteomics, Thiol labeling",

author = "Sophie Alvarez and Wilson, {Gordon H.} and Sixue Chen",

note = "Funding Information: Gordon Wilson is a high school junior sponsored by UF Center for Precollegiate Education Program. This work was supported by University of Florida and the National Science Foundation (MCB 76708). ",

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T1 - Determination of in vivo disulfide-bonded proteins in Arabidopsis

AU - Alvarez, Sophie

AU - Wilson, Gordon H.

AU - Chen, Sixue

N1 - Funding Information: Gordon Wilson is a high school junior sponsored by UF Center for Precollegiate Education Program. This work was supported by University of Florida and the National Science Foundation (MCB 76708).

PY - 2009/1/1

Y1 - 2009/1/1

N2 - 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.

AB - 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.

KW - Arabidopsis

KW - Disulfide bonds

KW - Mass spectrometry

KW - Proteomics

KW - Thiol labeling

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ER -

Determination of in vivo disulfide-bonded proteins in Arabidopsis

Abstract

Keywords

ASJC Scopus subject areas

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