Proteomic method for the quantification of methionine sulfoxide.
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.
Brock
J W C
JW
Department of Chemistry and Biochemistry, University of South Carolina, 631 Sumter St., Columbia, SC 29208, USA. brock@mail.chem.sc.edu
Cotham
W C
WC
Ames
J M
JM
Thorpe
S R
SR
Baynes
J W
JW
D000332:Aerobiosis; D002241:Carbohydrates; D006031:Glycosylation; D015227:Lipid Peroxidation; D008055:Lipids; D015416:Maillard Reaction; D013058:Mass Spectrometry; D008715:Methionine / Q000031:analogs & derivatives*; D010084:Oxidation-Reduction; D020543:Proteome; D017382:Reactive Oxygen Species; D012260:Ribonucleases / Q000737:chemistry
D002241:Carbohydrates; D008055:Lipids; D020543:Proteome; D017382:Reactive Oxygen Species; D008715:Methionine; D012260:Ribonucleases; C013111:methionine sulfoxide