Unit

UNIT 6.11 Measurement of Protein Glutathionylation

  1. Aleksandra Filipovska,
  2. Michael P. Murphy

Published Online: 1 JUN 2006

DOI: 10.1002/0471140856.tx0611s28

Current Protocols in Toxicology

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.

Author Information

  1. Medical Research Council, Dunn Human Nutrition Unit, Cambridge, United Kingdom

Publication History

  1. Published Online: 1 JUN 2006
  2. Published Print: MAY 2006

Abstract

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.

Keywords:

  • protein glutathionylation;
  • glutathione;
  • protein thiols;
  • oxidative stress;
  • redox regulation