Proteomic profile of reversible protein oxidation using PROP, purification of reversibly oxidized proteins.

ABSTRACT: Signal transduction pathways that are modulated by thiol oxidation events are beginning to be uncovered, but these discoveries are limited by the availability of relatively few analytical methods to examine protein oxidation compared to other signaling events such as protein phosphorylation. We report here the coupling of PROP, a method to purify reversibly oxidized proteins, with the proteomic identification of the purified mixture using mass spectrometry. A gene ontology (GO), KEGG enrichment and Wikipathways analysis of the identified proteins indicated a significant enrichment in proteins associated with both translation and mRNA splicing. This methodology also enabled the identification of some of the specific cysteine residue targets within identified proteins that are reversibly oxi

SUBMITTER: Victor KG 

PROVIDER: S-EPMC3289665 | biostudies-literature | 2012

REPOSITORIES: biostudies-literature