Proteomic method for the quantification of methionine sulfoxide.
Ann N Y Acad Sci
; 1043: 284-9, 2005 Jun.
Article
in En
| MEDLINE
| ID: mdl-16037250
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.
Search on Google
Collection:
01-internacional
Database:
MEDLINE
Main subject:
Proteome
/
Methionine
Language:
En
Journal:
Ann N Y Acad Sci
Year:
2005
Document type:
Article
Affiliation country: