Alpha-class isozymes of glutathione S-transferase in rat liver cytosol possess glutathione peroxidase activity toward phospholipid hydroperoxide.

Selenium-independent enzymes, found in the liver cytosol of selenium deficient rats, that are capable of reducing dilinoleoyl phosphatidylcholine hydroperoxide in the presence of reduced glutathione [Guan et al., (1995) Biochem. Mol. Biol. Int., 37, 1103-1110] were purified to homogeneity by use of successive chromatography on glutathione affinity and Mono P columns. The molecular weight of the purified protein was estimated by gel filtration to be approximately 50 kDa. Upon isoelectric focusing, the purified preparation showed two protein bands having pI values of 8.6 and 8.8. Both proteins had reactivity against both 1-chloro-2,4-dinitrobenzene and dilinoleoyl phosphatidylcholine hydroperoxide in the presence of reduced glutathione. Each of them consisted of two subunits having molecular weights of 24.3 kDa and 26 kDa, as estimated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. The large subunit was identified as rat glutathione S-transferase (GST) 2 (Yc subunit) based on the amino-terminal amino acid sequence analysis. The small subunit was considered to be most probably rat GST 1 (Ya subunit). From these results, we conclude that the basic alpha-class isozymes of GST in rat liver cytosol possess glutathione peroxidase activity toward phospholipid hydroperoxide.