Studies on the glutathione S-transferase activity associated with rat liver mitochondria.
The major proportion of rat liver glutathione S-transferase is cytosolic. Carefully washed mitochondria contain 0.25-0.47% of the cytosolic activity. Subfractionation of washed mitochondria using digitonin treatment revealed that glutathione S-transferase release did not parallel that of any of the mitochondrial marker enzymes. Glutathione S-transferase release paralleled that of lactate dehydrogenase, suggesting that these 'mitochondrial' activities are due to loosely bound cytoplasmic forms.
D000818:Animals; D002021:Buffers; D003600:Cytosol / Q000201:enzymology; D004072:Digitonin / Q000494:pharmacology; D005982:Glutathione Transferase / Q000378:metabolism*; D066298:In Vitro Techniques; D008297:Male; D008930:Mitochondria, Liver / Q000187:drug effects / Q000201:enzymology*; D051381:Rats; D011919:Rats, Inbred Strains; D013367:Submitochondrial Particles / Q000201:enzymology
D002021:Buffers; D005982:Glutathione Transferase; D004072:Digitonin