UNIT 6.11 Measurement of Protein Glutathionylation
Published Online: 1 JUN 2006
Copyright © 2006 by John Wiley & Sons, Inc.
Lab Protocol Title
Current Protocols in Toxicology
How to Cite
Filipovska, A. and Murphy, M. P. 2006. Measurement of Protein Glutathionylation. Current Protocols in Toxicology. 28:6.11:6.11.1–6.11.16.
- Published Online: 1 JUN 2006
- Published Print: MAY 2006
Proteins contain free, exposed thiols that can be glutathionylated in the native state as a result of thiol-disulfide exchange reactions with glutathione disulfide, catalyzed by glutaredoxin. A number of other reactions can also lead to protein glutathionylation. The modification of proteins by glutathionylation is important in oxidative damage and may be an important post-translational modification to proteins involved in redox signaling. This unit describes methods for the identification of glutathionylated proteins and quantification of the extent of glutathionylation. The protocols described use isolated mitochondrial protein complexes, mitochondrial membranes, and intact mitochondria, but can be easily adapted to other systems.
- protein glutathionylation;
- protein thiols;
- oxidative stress;
- redox regulation