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Proteomic Method for the Quantification of Methionine Sulfoxide
Author(s) -
BROCK J W C,
COTHAM W C,
AMES J M,
THORPE S R,
BAYNES J W
Publication year - 2005
Publication title -
annals of the new york academy of sciences
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.712
H-Index - 248
eISSN - 1749-6632
pISSN - 0077-8923
DOI - 10.1196/annals.1333.035
Subject(s) - maillard reaction , methionine sulfoxide , chemistry , methionine , biochemistry , sulfoxide , organic chemistry , amino acid
A bstract : 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 NaBH 4 , a commonly used reductant in the analysis of Maillard reaction products.