Summary
Recent studies indicate that protein glutathionylation is an important regulatory mechanism. The develop-ment of redox proteomics techniques to identify proteins undergoing glutathionylation has a key role in defining the importance of this post-translational modification, although the available methods are not yet comparable to those for the study of other modifications like phosphorylation. We describe here methods that have been successfully employed to identify in vitro glutathionylated proteins.
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Acknowledgments
Work supported in part by AFM and by MIUR (FIRB 2003), to EG, and Fondazione CARIPLO, Milano (to PG).
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Gianazza, E., Eberini, I., Ghezzi, P. (2009). Detection of Protein Glutathionylation. In: Tyther, R., Sheehan, D. (eds) Two-Dimensional Electrophoresis Protocols. Methods in Molecular Biology, vol 519. Humana Press. https://doi.org/10.1007/978-1-59745-281-6_26
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DOI: https://doi.org/10.1007/978-1-59745-281-6_26
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