Conversion of methionine to homocysteic acid in heavily oxidized proteomics samples

Details

Event Rapid Communications in Mass Spectrometry

Authors

Marshall Bern
Technical Publications
February 18th 2010
Analysis of protein oxidation is necessary in numerous areas of biochemistry, including hydroxyl radical surface mapping, oxidative stress assays, and pharmaceutical stability testing. Mass spectrometry is one of the tools most often used to identify protein oxidation products, and previous studies have attempted to identify and characterize all of the major oxidation products detected by mass spectrometry for each amino acid residue. In this note, we present evidence that in heavily oxidized protein samples, such as those produced by hydroxyl radical surface mapping, a major oxidation product of methionine is homocysteic acid. The formation of homocysteic acid from methionine was previously unrecognized in other mass spectrometric analyses, and has important implications for the analysis of oxidized samples, as well as potential implications as to the functional consequences of methionine oxidation.

Citation

Bern, M. W.; Saladino, J.; Sharp, J. Conversion of methionine to homocysteic acid in heavily oxidized proteomics samples. Rapid Communications in Mass Spectrometry. 2010 March 30; 24 (6): 768-772.

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