Proteomic method for the quantification of methionine sulfoxide

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

doi:10.1196/annals.1333.035

Proteomic method for the quantification of methionine sulfoxide

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

School of Biological Sciences

Research output: Contribution to journal › Article › peer-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 language	English
Pages (from-to)	284-289
Number of pages	6
Journal	Annals of the New York Academy of Sciences
Volume	1043
DOIs	https://doi.org/10.1196/annals.1333.035
Publication status	Published - 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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10.1196/annals.1333.035

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Cite this

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title = "Proteomic method for the quantification of methionine sulfoxide",

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.",

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AU - Brock, J.W.C.

AU - Cotham, W.C.

AU - Ames, Jennifer

AU - Thorpe, Suzanne

AU - Baynes, John

N1 - The Maillard Reaction: Chemistry at the Interface of Nutrition, Aging, and Disease

PY - 2005

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N2 - 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.

AB - 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.

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DO - 10.1196/annals.1333.035

M3 - Article

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JO - Annals of the New York Academy of Sciences

JF - Annals of the New York Academy of Sciences

SN - 1749-6632

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