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 spect...

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Veröffentlicht in:	Methods in Enzymology 2005, Vol.396, p.160-171
Hauptverfasser:	Kanski, Jaroslaw, Schöneich, Christian
Format:	Artikel
Sprache:	eng
Schlagworte:	Aging - metabolism Amino Acid Sequence Animals Antibody Specificity Chromatography, Affinity Chromatography, High Pressure Liquid Electrophoresis, Gel, Two-Dimensional Electrophoresis, Polyacrylamide Gel Immunoprecipitation Isoelectric Focusing Mass Spectrometry - methods Nitrates - metabolism Nitrosation Peptides - chemistry Proteins - chemistry Proteins - metabolism Rats
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Zusammenfassung:	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.
ISSN:	0076-6879 1557-7988
DOI:	10.1016/S0076-6879(05)96016-3