"Protein thiol redox plays an important role in numerous cellular processes and stress responses. The thiol moiety of cysteine residue is easily altered to various redox isoforms that play critical roles in regulation of both structure and function of proteins. In the present study, a quantitative thiol redox proteomic method, termed OxNSIL has been developed, which integrates the chemical labeling by biotin-tagged alkylating reagents with the heavy nitrogen stable isotope-coded salt metabolic labeling and acquires both advantages of biotin-avidin enrichment and MS-based quantitation of cysteine residue-containing peptides. Both the reduced and the reversibly oxidized cysteine thiol moieties are finally identified in a site-specific manner and measured in a single experiment.
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Citation: Hu Q, Guo G, Yang Z, Li Y, Xia Y (2014) Stable Isotope Metabolic Labeling-Based Quantitative Thiol Redox Proteomic Analysis of Hydrogen Peroxide-treated Arabidopsis plant. J Proteomics Bioinform 7: 121-133."
Last date updated on December, 2020