期刊
JOURNAL OF PROTEOME RESEARCH
卷 19, 期 2, 页码 624-633出版社
AMER CHEMICAL SOC
DOI: 10.1021/acs.jproteome.9b00505
关键词
methionine oxidation; redox chemistry; hydrogen peroxide; oxidative protein damage; quantitative proteomics
资金
- National Institutes of Health [R35 GM119502, 15100D021486-01, 1S10OD025242-01]
The oxidation of methionine is an important post-translational modification of proteins with numerous roles in physiology and pathology. However, the quantitative analysis of methionine oxidation on a proteome-wide scale has been hampered by technical limitations. Methionine is readily oxidized in vitro during sample preparation and analysis. In addition, there is a lack of enrichment protocols for peptides that contain an oxidized methionine residue, making the accurate quantification of methionine oxidation difficult to achieve on a global scale. Herein, we report a methodology to circumvent these issues by isotopically labeling unoxidized methionines with O-18-labeled hydrogen peroxide and quantifying the relative ratios of O-18- and O-16-oxidized methionines. We validate our methodology using artificially oxidized proteomes made to mimic varying degrees of methionine oxidation. Using this method, we identify and quantify a number of novel sites of in vivo methionine oxidation in an unstressed human cell line.
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