Glutathione transferases in primary rat hepatomas: the isolation of a form with GSH peroxidase activity.
A previously uncharacterized glutathione (GSH) transferase which is not apparent in normal liver, accounts for at least 25% of the soluble GSH transferase content of primary hepatomas induced by feeding N,N-dimethyl-4-aminoazobenzene. This enzyme is readily isolated, has an isoelectric point of 6.8, is composed of two identical subunits of apparent Mr 26000 and has GSH transferase activity towards a number of substrates including benzo(a)pyrene-7,8-diol-9,10-oxide. It is unusual in that it has GSH peroxidase activity towards fatty acid hydroperoxides but not towards the model substrates, cumene hydroperoxide and t-butyl hydroperoxide. It has been shown by tryptic peptide analysis to be distinct from GSH transferases composed of subunits 1, 2, 3, 4 or 6 and has been designated GSH transferase 7-7.
D000818:Animals; D005979:Glutathione Peroxidase / Q000032:analysis*; D005982:Glutathione Transferase / Q000032:analysis* / Q000302:isolation & purification; D008114:Liver Neoplasms, Experimental / Q000201:enzymology*; D008297:Male; D051381:Rats; D011919:Rats, Inbred Strains
D005979:Glutathione Peroxidase; D005982:Glutathione Transferase