title: Novel method to investigate protein carbonylation by iTRAQ strategy.
abstract: This paper reports a novel methodology for relative quantitative analysis of carbonylation sites in proteins by exploiting a new isobaric tag for relative and absolute quantitation (iTRAQ) derivative, iTRAQ hydrazide (iTRAQH), and the analytical power of linear ion trap instruments (QqLIT). Because of its operational simplicity, avoiding time-consuming enrichment procedures, this new strategy seems to be well suited for quantitative large-scale proteomic profiling of carbonylation.
authors.affiliation: Dipartimento di Scienze Chimiche, Università di Napoli Federico II, Naples, Italy.
authors.forename: Angelo
authors.initials: A
authors.lastname: Palmese
authors.forename: Chiara
authors.initials: C
authors.lastname: De Rosa
authors.forename: Giovanni
authors.initials: G
authors.lastname: Chiappetta
authors.forename: Gennaro
authors.initials: G
authors.lastname: Marino
authors.forename: Angela
authors.initials: A
authors.lastname: Amoresano
mesh_terms: D050050:Protein Carbonylation; D011506:Proteins / Q000737:chemistry*; D040901:Proteomics; D019032:Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization / Q000379:methods; D053719:Tandem Mass Spectrometry / Q000379:methods*
chemical_list: D011506:Proteins