Protein nitration in biological aging: proteomic and tandem mass spectrometric characterization of nitrated sites.
Proteomic techniques for the identification of 3-nitrotyrosine-containing proteins in various biological systems are described with emphasis on the direct mass spectrometric detection and sequencing of 3-nitrotyrosine-containing peptides. Strengths and weaknesses of various separation and mass spectrometric techniques are discussed. Some examples for the MS/MS analysis of nitrated peptides obtained from aging rat heart and skeletal muscle are provided, such as nitration of Tyr105 of the mitochondrial electron-transfer flavoprotein and Tyr14 of creatine kinase.
Kanski
Jaroslaw
J
Department of Pharmaceutical Chemistry, University of Kansas, Lawrence, Kansas 66047, USA.
Schöneich
Christian
C
D000375:Aging / Q000378:metabolism*; D000595:Amino Acid Sequence; D000818:Animals; D000918:Antibody Specificity; D002846:Chromatography, Affinity; D002851:Chromatography, High Pressure Liquid; D015180:Electrophoresis, Gel, Two-Dimensional; D004591:Electrophoresis, Polyacrylamide Gel; D047468:Immunoprecipitation; D007525:Isoelectric Focusing; D013058:Mass Spectrometry / Q000379:methods; D009566:Nitrates / Q000378:metabolism*; D015538:Nitrosation; D010455:Peptides / Q000737:chemistry; D011506:Proteins / Q000737:chemistry / Q000378:metabolism*; D051381:Rats
D009566:Nitrates; D010455:Peptides; D011506:Proteins