Peer-Reviewed Journal Details
Mandatory Fields
McDonagh, B; Martínez-Acedo, P: Vázquez, J; Padilla, CA; Sheehan, D; Bárcena, JA
2012
Unknown
Journal Of Proteomics
Application of iTRAQ Reagents to Relatively Quantify the Reversible Redox State of Cysteine Residues.
Published
()
Optional Fields
Redox proteomics
514847
2012
54187
54196
Cysteines are one of the most rarely used amino acids, but when conserved in proteins they often play critical roles in structure, function, or regulation. Reversible cysteine modifications allow for potential redox regulation of proteins. Traditional measurement of the relative absolute quantity of a protein between two samples is not always necessarily proportional to the activity of the protein. We propose application of iTRAQ reagents in combination with a previous thiol selection method to relatively quantify the redox state of cysteines both within and between samples in a single analysis. Our method allows for the identification of the proteins, identification of redox-sensitive cysteines within proteins, and quantification of the redox status of individual cysteine-containing peptides. As a proof of principle, we applied this technique to yeast alcohol dehydrogenase-1 exposed in vitro to H(2)O(2) and also in vivo to the complex proteome of the Gram-negative bacterium Bacillus subtilis.
3403169
https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3403169/
10.1155/2012/514847
Grant Details
Publication Themes
Biomedical Science and Engineering