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Proteomic method for the quantification of methionine sulfoxide

Brock, 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

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To link to this item DOI: 10.1196/annals.1333.035

Abstract/Summary

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.

Item Type:Book or Report Section
Divisions:Faculty of Life Sciences > School of Chemistry, Food and Pharmacy > Department of Food and Nutritional Sciences
ID Code:13538
Uncontrolled Keywords:methionine sulfoxide, glycoxidation, lipoxidation, proteomics, protein mass spectrometry , OXIDATIVE STRESS, PROTEINS, RESIDUES, REDUCTION, GLYCATION, MECHANISM
Additional Information:8th International Symposium on the Maillard Reaction Charleston, SC, AUG 29-SEP 01, 2004
Publisher:New York Academy of Sciences

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