## Abstract | I. | Introduction | 260 | | II. | Progress on Mapping Organellar Proteomes and Their Component Protein Complexes | 260 | | | A. Mitochondria | 260 | | | 1. Global Analysis | 260 | | | 2. Directed Analysis | 262 | | | 3. Protein Complexes | 263 | | | a.
Mass spectrometry-based survey of age-associated protein carbonylation in rat brain mitochondria
✍ Scribed by Laszlo Prokai; Liang-Jun Yan; José L. Vera-Serrano; Stanley M. Stevens Jr; Michael J. Forster
- Publisher
- John Wiley and Sons
- Year
- 2007
- Tongue
- English
- Weight
- 282 KB
- Volume
- 42
- Category
- Article
- ISSN
- 1076-5174
- DOI
- 10.1002/jms.1345
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✦ Synopsis
Abstract
There is a body of evidence lending credence to the idea that oxidative stress may be responsible for age‐related deleterious changes in brain function, and that protein carbonylation is a potential marker for such changes. An investigation of oxidative damage to mitochondrial proteins from aged rat brains was done using gel electrophoresis coupled with carbonylation‐specific immunostaining. Six proteins that appeared to be susceptible to oxidative modification were identified by in‐gel trypsin digestion followed by matrix‐assisted laser desorption/ionization mass spectrometry and tandem mass spectrometry. Two subunits of the H^+^‐transporting ATP synthase, adenine nucleotide translocator, voltage‐dependent anion channel, glutamate oxaloacetate transaminase, and aconitase were identified as likely targets of age‐associated carbonylation. Copyright © 2007 John Wiley & Sons, Ltd.
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