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Quantitative Proteomics Using Reductive Dimethylation for Stable Isotope Labeling
Published on: July 1, 2014
Proteomic method for the quantification of methionine sulfoxide
J W C Brock1, W C Cotham, J M Ames
1Department of Chemistry and Biochemistry, University of South Carolina, 631 Sumter St., Columbia, SC 29208, USA. brock@mail.chem.sc.edu
Annals of the New York Academy of Sciences
|July 23, 2005
Summary
This study introduces a proteomic method to analyze methionine oxidation (MetSO) in proteins. Researchers measured MetSO formation and its reduction, offering new insights into the Maillard reaction.
Area of Science:
- Biochemistry
- Proteomics
- Chemical Biology
Background:
- Glycoxidation and lipoxidation are key reactions in the Maillard reaction, leading to protein modification.
- Reactive oxygen species generated during these processes cause irreversible protein oxidation.
- Methionine residues are particularly vulnerable to oxidation, forming methionine sulfoxide (MetSO).
Purpose of the Study:
- To develop and present a novel proteomic method for quantifying MetSO in proteins.
- To investigate MetSO formation in a model protein (RNase) under specific oxidative conditions.
- To assess the susceptibility of MetSO to reduction by sodium borohydride (NaBH4).
Main Methods:
- Proteomic techniques were employed for the analysis of MetSO.
- The model protein RNase was incubated aerobically with glucose and arachidonate.
- Formation of MetSO and its reduction by NaBH4 were measured.
Main Results:
- The study successfully measured MetSO formation on RNase.
- The method allowed for the quantification of MetSO under aerobic incubation with glucose and arachidonate.
- The susceptibility of MetSO to reduction by NaBH4 was evaluated.
Conclusions:
- A reliable proteomic method for MetSO analysis has been established.
- The findings provide quantitative data on MetSO formation during Maillard-related oxidative processes.
- The study contributes to understanding protein oxidation and potential reduction strategies.
