Purification of proteins susceptible to oxidation at cysteine residues: identification of malate dehydrogenase as a target for S-glutathiolation.
The cysteine residues of proteins are susceptible to a range of oxidative modifications, including S-glutathiolation. Here we present a study in which we used glutathione-agarose to purify cardiac proteins that undergo S-glutathiolation during oxidative stress. We then identified one of the oxidized proteins as malate dehydrogenase.
Eaton
Philip
P
The Centre for Cardiovascular Biology and Medicine, The Rayne Institute, King's College London, London, SE1 7EH, UK. p.eaton@kcl.ac.uk
Shattock
Michael J
MJ
D000818:Animals; D002846:Chromatography, Affinity; D003545:Cysteine / Q000378:metabolism*; D005978:Glutathione / Q000378:metabolism*; D008291:Malate Dehydrogenase / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism*; D009206:Myocardium / Q000201:enzymology*; D010084:Oxidation-Reduction; D011499:Protein Processing, Post-Translational; D051381:Rats
D008291:Malate Dehydrogenase; D005978:Glutathione; D003545:Cysteine