Measurement of protein glutathionylation.

TitleMeasurement of protein glutathionylation.
Publication TypeJournal Article
Year of Publication2006
AuthorsFilipovska, A, Murphy, MP
JournalCurr Protoc Toxicol
VolumeChapter 6
PaginationUnit6.11
Date Published2006 Jun
ISSN1934-9262
KeywordsAnimals, Cattle, Glutathione, Mitochondria, Heart, Proteins, Sulfur Radioisotopes
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.

DOI10.1002/0471140856.tx0611s28
Alternate JournalCurr Protoc Toxicol
Citation Key10.1002/0471140856.tx0611s28
PubMed ID23045137