Abstract
The redox proteomics technique normally combines two-dimensional gel electrophoresis, mass spectrometry, and protein databases to analyze the cell proteome from various samples, thereby leading to the identification of specific targets of oxidative modification. Oxidative stress that occurs because of increased levels of reactive oxygen species and reactive nitrogen species can target most biomolecules, consequently leading to altered physiological function of the cells. Redox proteomics has identified oxidatively modified protein targets in various pathological conditions, consequently providing insight into the pathways involved in the pathogenesis of these conditions. This approach also can be used to identify possible protective mechanisms to prevent or delay these disorders.
Original language | English |
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Pages (from-to) | 487-494 |
Number of pages | 8 |
Journal | Free Radical Biology and Medicine |
Volume | 50 |
Issue number | 4 |
DOIs | |
State | Published - Feb 15 2011 |
Bibliographical note
Funding Information:This research was supported by a NIH grant to D.A.B. (AG-05119).
Funding
This research was supported by a NIH grant to D.A.B. (AG-05119).
Funders | Funder number |
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National Institutes of Health (NIH) | AG-05119 |
Keywords
- 3-Nitrotyrosine
- Mass spectrometry
- Oxidative modification
- Protein carbonyls
- Protein-bound HNE
- Redox proteomics
- Two-dimensional gel electrophoresis
ASJC Scopus subject areas
- Biochemistry
- Physiology (medical)