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Related Experiment Video

Updated: May 23, 2026

Profiling Thiol Redox Proteome Using Isotope Tagging Mass Spectrometry
12:07

Profiling Thiol Redox Proteome Using Isotope Tagging Mass Spectrometry

Published on: March 24, 2012

Profiling thiol redox proteome using isotope tagging mass spectrometry.

Jennifer Parker1, Ning Zhu, Mengmeng Zhu

  • 1Plant Molecular and Cellular Biology Program, University of Florida, Florida, USA.

Journal of Visualized Experiments : Jove
|April 5, 2012
PubMed
Summary

Pseudomonas syringae pv. tomato (Pst DC3000) infection in tomato leaves involves reactive oxygen species (ROS). This study used cysteine-reactive tandem mass tag (cysTMT) technology to analyze redox proteomic changes in tomato leaves during Pst DC3000 infection.

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Last Updated: May 23, 2026

Profiling Thiol Redox Proteome Using Isotope Tagging Mass Spectrometry
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Published on: March 24, 2012

Resin-Assisted Capture Coupled with Isobaric Tandem Mass Tag Labeling for Multiplexed Quantification of Protein Thiol Oxidation
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Quantitative Proteomics Using Reductive Dimethylation for Stable Isotope Labeling
11:53

Quantitative Proteomics Using Reductive Dimethylation for Stable Isotope Labeling

Published on: July 1, 2014

Area of Science:

  • Plant Pathology
  • Proteomics
  • Biochemistry

Background:

  • Pseudomonas syringae pv. tomato (Pst DC3000) causes bacterial speck disease in tomato (Solanum lycopersicum).
  • Reactive oxygen species (ROS), including hydrogen peroxide, accumulate in infected plant tissues and play a role in disease development.
  • Cysteine residues in proteins are sensitive to redox changes and act as critical signaling molecules.

Purpose of the Study:

  • To investigate the redox proteomic changes in tomato leaves upon infection with Pst DC3000.
  • To apply cysteine-reactive tandem mass tag (cysTMT) technology for high-throughput redox proteomic analysis.

Main Methods:

  • Tomato (Rio Grande) leaves were inoculated with Pst DC3000.
  • Cysteine-reactive tandem mass tag (cysTMT) reagents were used for selective labeling of cysteine-containing peptides.
  • Protease digestion and enrichment of labeled peptides were performed.
  • Tandem mass spectrometry (MS/MS) was employed for quantitative analysis of protein redox states.

Main Results:

  • The study successfully applied cysTMT technology to analyze redox proteomic changes in Pst DC3000-infected tomato leaves.
  • This method allowed for the relative quantitation of cysteine modifications in response to bacterial infection.

Conclusions:

  • CysTMT technology provides a powerful, high-throughput approach for studying redox proteomics in plants.
  • This methodology can be utilized to explore redox-regulated physiological processes in response to various stresses, including pathogen infection.