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Mass spectrometry‐based survey of age‐associated protein carbonylation in rat brain mitochondria
Author(s) -
Prokai Laszlo,
Yan LiangJun,
VeraSerrano José L.,
Stevens Stanley M.,
Forster Michael J.
Publication year - 2007
Publication title -
journal of mass spectrometry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.475
H-Index - 121
eISSN - 1096-9888
pISSN - 1076-5174
DOI - 10.1002/jms.1345
Subject(s) - chemistry , protein carbonylation , aconitase , carbonylation , oxidative phosphorylation , mass spectrometry , biochemistry , oxidative stress , mitochondrion , peptide mass fingerprinting , adenine nucleotide translocator , chromatography , proteomics , oxidative damage , carbon monoxide , gene , catalysis
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.