Multiple forms of glutathione S-transferase from pig liver--reaction with methyl linoleate hydroperoxides

1. Seven isoenzyme forms of glutathione S-transferase were purified from pig liver. 2. The most basic isoenzyme reduced methyl 13-hydroperoxy-cis-9,trans-11-octadecadienoate in the absence of detergent at a higher rate (0.3 mumol/min/mg protein) than predicted from substrate solubility. 3. This demonstrates that glutathione transferase possesses some surface acting character for neutral lipid hydroperoxides.