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Updated: Jun 12, 2026

Resin-Assisted Capture Coupled with Isobaric Tandem Mass Tag Labeling for Multiplexed Quantification of Protein Thiol Oxidation

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A simple method to systematically study oxidatively modified proteins in biological samples and its applications.

Byoung-Joon Song¹, Soo-Kyung Suh, Kwan-Hoon Moon

¹Laboratory of Membrane Biochemistry and Biophysics, National Institute on Alcohol Abuse and Alcoholism, Bethesda, Maryland, USA.

Methods in Enzymology

|June 2, 2010

Summary

Oxidative stress from reactive oxygen/nitrogen species (ROS/RNS) impacts disease. This study details a method to identify oxidized proteins, crucial for understanding their role in ER stress and organ damage.

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Enabling Real-Time Compensation in Fast Photochemical Oxidations of Proteins for the Determination of Protein Topography Changes

Enabling Real-Time Compensation in Fast Photochemical Oxidations of Proteins for the Determination of Protein Topography Changes

Published on: September 1, 2020

Area of Science:

Biochemistry
Molecular Biology
Pathophysiology

Background:

Oxidative stress, characterized by elevated reactive oxygen/nitrogen species (ROS/RNS), is implicated in numerous diseases.
While oxidized DNA and lipids are well-studied, oxidative modifications in proteins remain less understood due to methodological challenges.
Challenges include the need for specific reagents, difficulties in detection and purification, and limitations of early analytical instruments.

Purpose of the Study:

To present a detailed procedure for systematically identifying oxidatively modified proteins in biological samples.
To highlight the functional significance of these modifications in disease pathogenesis.
To provide insights into the role of oxidized proteins in endoplasmic reticulum (ER) stress and mitochondrial dysfunction.

Main Methods:

Detailed procedural description for the systematic identification of oxidatively modified proteins.
Utilizes advanced analytical techniques for sensitive detection and purification.
Focuses on biological samples to ensure relevance to disease states.

Main Results:

A comprehensive method for identifying oxidatively modified proteins is established.
The method facilitates understanding the functional consequences of protein oxidation.
Demonstrates the link between oxidized proteins and cellular dysfunction.

Conclusions:

The developed method enables systematic identification of oxidatively modified proteins.
Understanding protein oxidation is key to elucidating disease mechanisms.
This approach aids in studying the contribution of oxidized proteins to ER stress, mitochondrial dysfunction, and organ damage.