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

Search research articles

Related Experiment Video

Updated: Jun 16, 2026

Capillary Electrophoresis Mass Spectrometry Approaches for Characterization of the Protein and Metabolite Corona Acquired by Nanomaterials

Capillary Electrophoresis Mass Spectrometry Approaches for Characterization of the Protein and Metabolite Corona Acquired by Nanomaterials

Published on: October 27, 2020

Profiling carbonylated proteins in human plasma.

Ashraf G Madian¹, Fred E Regnier

¹Department of Chemistry, Purdue University, West Lafayette, Indiana 47907, USA.

Journal of Proteome Research

|February 4, 2010

Summary

This summary is machine-generated.

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

Mobile Affinity Selection Chromatography Analysis of Therapeutic Monoclonal Antibodies.

Analytical chemistry·2023

Same author

Mobile Affinity Sorbent Chromatography.

Analytical chemistry·2017

Same author

Proteins and Proteoforms: New Separation Challenges.

Analytical chemistry·2017

Same author

Identification of Novel Protein Expression Changes Following Cisplatin Treatment and Application to Combination Therapy.

Journal of proteome research·2017

Same author

Large-Scale Interlaboratory Study to Develop, Analytically Validate and Apply Highly Multiplexed, Quantitative Peptide Assays to Measure Cancer-Relevant Proteins in Plasma.

Molecular & cellular proteomics : MCP·2015

Same author

Redox proteomic investigation of tetracycline-induced steatosis.

Proteomics·2014

This study identifies oxidized proteins in human plasma using proteomics. It reveals diverse oxidative modifications and their origins, offering new insights into protein damage mechanisms.

Area of Science:

Biochemistry
Proteomics
Mass Spectrometry

Background:

Oxidative stress contributes to various diseases.
Identifying oxidized proteins in plasma is crucial for understanding disease mechanisms.
Previous methods lacked comprehensive identification of diverse oxidative modifications.

Purpose of the Study:

To identify and characterize oxidized proteins in human plasma.
To map various oxidative modifications on specific proteins.
To differentiate biological mechanisms of protein oxidation.

Main Methods:

Proteomic analysis of carbonylated proteins isolated from human plasma.
Avidin affinity chromatography and biotinylation for protein isolation.
Peptide digestion, separation by chromatography, and identification by mass spectrometry (electrospray ionization and MALDI-TOF).

More Related Videos

Standardized SDS-PAGE Workflow for Personalized Protein Corona Profiling in Early Cancer Detection

Standardized SDS-PAGE Workflow for Personalized Protein Corona Profiling in Early Cancer Detection

Published on: December 19, 2025

Related Experiment Videos

Last Updated: Jun 16, 2026

Capillary Electrophoresis Mass Spectrometry Approaches for Characterization of the Protein and Metabolite Corona Acquired by Nanomaterials

Capillary Electrophoresis Mass Spectrometry Approaches for Characterization of the Protein and Metabolite Corona Acquired by Nanomaterials

Published on: October 27, 2020

Standardized SDS-PAGE Workflow for Personalized Protein Corona Profiling in Early Cancer Detection

Standardized SDS-PAGE Workflow for Personalized Protein Corona Profiling in Early Cancer Detection

Published on: December 19, 2025

Main Results:

Identified 65 high, medium, and low abundance oxidized proteins in human plasma.
Detected 24 oxidative modifications across 14 proteins, including methionine and tryptophan oxidation.
Apolipoprotein B-100 exhibited the highest number of oxidative modifications (20).
Differentiated oxidation products from reactive oxygen species, advanced glycation endproducts (AGEs), and lipid peroxidation.

Conclusions:

This study provides the first proteomic identification of oxidized proteins in human plasma.
Mass spectrometry enabled the simultaneous recognition of multiple oxidation pathways.
Findings advance the understanding of protein oxidation mechanisms and their biological implications.