Proteomic method for the quantification of methionine sulfoxide

J.W.C. Brock, W.C. Cotham, Jennifer Ames, Suzanne Thorpe, John Baynes

Research output: Contribution to journalArticlepeer-review

8 Citations (Scopus)

Abstract

Glycoxidation and lipoxidation reactions contribute to the chemical modification of proteins during the Maillard reaction. Reactive oxygen species, produced during the oxidation of sugars and lipids in these processes, irreversibly oxidize proteins. Methionine is particularly susceptible to oxidation, yielding the oxidation product methionine sulfoxide (MetSO). Here we describe a method for the analysis of MetSO using proteomic techniques. Using these techniques, we measured MetSO formation on the model protein RNase during aerobic incubations with glucose and arachidonate. We also evaluated the susceptibility of MetSO to reduction by NaBH4, a commonly used reductant in the analysis of Maillard reaction products.
Original languageEnglish
Pages (from-to)284-289
Number of pages6
JournalAnnals of the New York Academy of Sciences
Volume1043
DOIs
Publication statusPublished - 2005

Bibliographical note

The Maillard Reaction: Chemistry at the Interface of Nutrition, Aging, and Disease

ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)

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