Proteomic method for the quantification of methionine sulfoxideBrock, J.W.C., Cotham, W.C., Ames, J.M., Thorpe, S.R. and Baynes, J.W. (2005) Proteomic method for the quantification of methionine sulfoxide. In: Baynes, J.W., Thorpe, S.R. , Monnier, V.M. and Ames, J.M. (eds.) Maillard reaction: chemistry at the interface of nutrition, aging and disease. Annals of the New York Academy of Sciences, 1043. New York Academy of Sciences, New York, pp. 284-289. ISBN 9781573315326 Full text not archived in this repository. It is advisable to refer to the publisher's version if you intend to cite from this work. See Guidance on citing. To link to this item DOI: 10.1196/annals.1333.035 Abstract/SummaryGlycoxidation 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.
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