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.
Modification of alpha-aminoadipic semialdehyde by a novel iTRAQ reagent, namely iTRAQ-hydrazide; by using this reagent it is possible to selectively label carbonylated residues in order to perform qualitative and quantitative analysis of protein carbonylation.
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Palmese, A., De Rosa, C., Chiappetta, G. et al. Novel method to investigate protein carbonylation by iTRAQ strategy. Anal Bioanal Chem 404, 1631–1635 (2012). https://doi.org/10.1007/s00216-012-6324-9
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DOI: https://doi.org/10.1007/s00216-012-6324-9