Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
1910737 | Free Radical Biology and Medicine | 2009 | 6 Pages |
Abstract
The oxidative modification of proteins is believed to play a critical role in the etiology and/or progression of several diseases. α-Aminoadipic semialdehyde (AAS) and γ-glutamic semialdehyde (GGS) residues represent major oxidized amino acids generated in oxidized proteins. This paper describes a novel procedure for the specific and sensitive determination of AAS and GGS after their reductive amination with sodium cyanoborohydride and p-aminobenzoic acid, a fluorescence reagent, to their corresponding derivatives, followed by a high-performance liquid chromatography (HPLC) analysis. This fluorescent labeling of protein-associated aldehyde moieties is a simple and accurate technique that may be widely used to reveal increased levels of oxidatively modified proteins with reactive oxygen species during aging and disease.
Keywords
PBSGGSγ-Glutamic semialdehydeDNPHAASMCOSDSABADTPA2-(N-morpholino)ethanesulfonic acid2,4-dinitrophenylhydrazineBSAGC/MSP-aminobenzoic acidbovine serum albuminHacAMetal-catalyzed oxidationPhosphate-buffered salineMeSα-Aminoadipic semialdehydeHPLChigh-performance liquid chromatographygas chromatography/mass spectrometry
Related Topics
Life Sciences
Biochemistry, Genetics and Molecular Biology
Ageing
Authors
Mitsugu Akagawa, Kyozo Suyama, Koji Uchida,