Search research articles

ABOUT JoVE

Overview Leadership Blog JoVE Help Center

AUTHORS

Publishing Process Editorial Board Scope & Policies Peer Review FAQ Submit

LIBRARIANS

Testimonials Subscriptions Access Resources Library Advisory Board FAQ

RESEARCH

JoVE Journal Methods Collections JoVE Encyclopedia of Experiments Archive

EDUCATION

JoVE Core JoVE Business JoVE Science Education JoVE Lab Manual Faculty Resource Center Faculty Site

Terms & Conditions of Use

Related Concept Videos

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by

Same author

ProteoMeter: a pipeline for integrating multi-PTM and limited proteolysis data to reveal modification-structure coupling at the residue level.

NAR genomics and bioinformatics·2026

Same author

Interlaboratory Comparison of a Glucagon and Oxyntomodulin Immuno-LC-MS/MS Assay: Implications for Diabetes Research.

Clinical chemistry·2026

Same author

Phosphoproteomics in Vascular Biology and Disease: Illuminating Signaling in the Vessel.

Arteriosclerosis, thrombosis, and vascular biology·2026

Same author

A multiplexed targeted mass spectrometric assay for quantifying obesity- associated biomarkers in human plasma.

Research square·2026

Same author

Aggregation Methods for Quantifying PTM and Structural Changes in Bottom-Up Proteomics.

Journal of proteome research·2026

Same author

Thiol post-translational modifications modulate allosteric regulation of the OpcA-G6PDH complex through conformational gate control.

Protein science : a publication of the Protein Society·2026

Search research articles

Related Experiment Video

Updated: Jul 5, 2026

Nitropeptide Profiling and Identification Illustrated by Angiotensin II

Nitropeptide Profiling and Identification Illustrated by Angiotensin II

Published on: June 16, 2019

Quantitative proteome mapping of nitrotyrosines.

Diana J Bigelow¹, Wei-Jun Qian

¹Cell Biology and Biochemistry Group, Division of Biological Sciences, Pacific Northwest National Laboratory, Richland, Washington, USA.

Methods in Enzymology

|April 22, 2008

Summary

Early detection of nitrotyrosine, an inflammatory marker, is crucial for understanding disease. Liquid chromatography coupled with tandem mass spectrometry (LC-MS/MS) enables proteome-wide quantitation of nitrotyrosine for disease biomarker discovery and therapeutic strategies.

More Related Videos

Integration of Miniaturized Solid Phase Extraction and LC-MS/MS Detection of 3-Nitrotyrosine in Human Urine for Clinical Applications

Integration of Miniaturized Solid Phase Extraction and LC-MS/MS Detection of 3-Nitrotyrosine in Human Urine for Clinical Applications

Published on: July 14, 2017

Detection of 3-Nitrotyrosine in Atmospheric Environments via a High-performance Liquid Chromatography-electrochemical Detector System

Detection of 3-Nitrotyrosine in Atmospheric Environments via a High-performance Liquid Chromatography-electrochemical Detector System

Published on: January 30, 2019

Related Experiment Videos

Last Updated: Jul 5, 2026

Nitropeptide Profiling and Identification Illustrated by Angiotensin II

Nitropeptide Profiling and Identification Illustrated by Angiotensin II

Published on: June 16, 2019

Integration of Miniaturized Solid Phase Extraction and LC-MS/MS Detection of 3-Nitrotyrosine in Human Urine for Clinical Applications

Integration of Miniaturized Solid Phase Extraction and LC-MS/MS Detection of 3-Nitrotyrosine in Human Urine for Clinical Applications

Published on: July 14, 2017

Detection of 3-Nitrotyrosine in Atmospheric Environments via a High-performance Liquid Chromatography-electrochemical Detector System

Detection of 3-Nitrotyrosine in Atmospheric Environments via a High-performance Liquid Chromatography-electrochemical Detector System

Published on: January 30, 2019

Area of Science:

Biochemistry
Proteomics
Biomarker Discovery

Background:

Increased nitrotyrosine levels serve as an early indicator of disease and environmental stress.
Quantitative analysis of nitrotyrosine and related oxidative modifications is vital for identifying disease risk and progression.
Understanding these modifications is key to developing effective therapeutic strategies.

Purpose of the Study:

To discuss the application of liquid chromatography coupled with tandem mass spectrometry (LC-MS/MS) for the quantitation and identification of nitrotyrosine-modified proteins.
To highlight the utility of LC-MS/MS in analyzing complex mammalian proteomes for oxidative modifications.
To underscore the importance of nitrotyrosine detection in disease research.

Main Methods:

Multidimensional separation techniques, specifically liquid chromatography (LC).
Tandem mass spectrometry (MS/MS) for protein identification and quantitation.
Application of LC-MS/MS to complex protein mixtures within mammalian proteomes.

Main Results:

LC-MS/MS has significantly advanced the study of mammalian proteomes.
This technique facilitates the identification of posttranslational modifications, including nitrotyrosine.
The study focuses on the quantitation and identification of nitrotyrosine-modified proteins.

Conclusions:

LC-MS/MS is a powerful tool for the proteome-wide quantitation of nitrotyrosine.
This methodology aids in the early detection of disease biomarkers and progression.
The findings support the use of LC-MS/MS for identifying oxidative modifications in complex biological samples.