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604873 
Journal Article 
Protein thiol oxidation in health and disease: Techniques for measuring disulfides and related modifications in complex protein mixtures 
Eaton, P 
2006 
Yes 
Free Radical Biology and Medicine
ISSN: 0891-5849
EISSN: 1873-4596 
40 
11 
1889-1899 
Abstract: Oxidant species are known to contribute to disease and dysfunction in biological systems. However, evidence has been progressively accumulating that demonstrates a more fundamental role for many oxidant species in the regulation of everyday function of healthy cells. Redox dependent signaling events involving the post-translational, oxidative modification of proteins has now been accepted as an important regulatory process, although the full extent of such mechanisms is yet to be determined. Some protein cysteinyl thiols are known to be susceptible to a number of redox-dependent modifications, including an interchange between the reduced thiol and several different oxidized disulfide states. Here, the role of oxidants as regulatory entities is reviewed, as are the many different ways protein disulfide formation can be analysed in complex protein mixtures. This includes an overview of many of the Proteomic strategies that can be used to identify proteins that form disulfides when pro-oxidizing conditions arise in cells, as well as related methods for studying intermediates that may precede disulfide formation. [Copyright 2006 Elsevier] Copyright of Free Radical Biology & Medicine is the property of Elsevier Science Publishing Company, Inc. and its content may not be copied or emailed to multiple sites or posted to a listserv without the copyright holder's express written permission. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.) 
OXIDATION; GLUTATHIONE; ENZYME-linked immunosorbent assay; GEL electrophoresis; 4-nitrobenzyl chloride ( NBD-Cl ); 5; 5′-dithiobis-2-nitrobenzoic acid ( DTNB ); 5,5′-dithiobis-2-nitrobenzoic acid ( DTNB ); dithiothreitol ( DTT ); enzyme linked immunosorbent assay ( ELISA ); glutathione disulfide ( GSSG ); isoelectric focusing ( IEF ); isotope-coded affinity tagging ( ICAT ); isotopic tag for absolute and relative quantitation ( IRAQ ); N-ethylmaleimide ( NEM ); reduced glutathione ( GSH ); S-nitrosoglutathione ( GSNO ); sodium dodecyl sulfate–polyacrylamide gel electrophoresis ( SDS-PAGE )