Proteomic method for the quantification of methionine sulfoxide


Autoria(s): Brock, J.W.C.; Cotham, W.C.; Ames, Jennifer; Thorpe, Suzanne; Baynes, John
Data(s)

2005

Resumo

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.

Identificador

http://pure.qub.ac.uk/portal/en/publications/proteomic-method-for-the-quantification-of-methionine-sulfoxide(aea164fd-400c-4be5-b531-287fb3870436).html

http://dx.doi.org/10.1196/annals.1333.035

http://www.scopus.com/inward/record.url?scp=23744460952&partnerID=8YFLogxK

Idioma(s)

eng

Direitos

info:eu-repo/semantics/restrictedAccess

Fonte

Brock , J W C , Cotham , W C , Ames , J , Thorpe , S & Baynes , J 2005 , ' Proteomic method for the quantification of methionine sulfoxide ' MAILLARD REACTION: CHEMISTRY AT THE INTERFACE OF NUTRITION, AGING, AND DISEASE , vol 1043 , pp. 284-289 . DOI: 10.1196/annals.1333.035

Palavras-Chave #/dk/atira/pure/subjectarea/asjc/1300 #Biochemistry, Genetics and Molecular Biology(all)
Tipo

article