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.
Williamson
G
G
AFRC Institute of Food Research, Norwich Laboratory, England.
D000818:Animals; D002851:Chromatography, High Pressure Liquid; D003902:Detergents / Q000494:pharmacology; D005982:Glutathione Transferase / Q000302:isolation & purification* / Q000378:metabolism; D007527:Isoenzymes / Q000302:isolation & purification*; D007700:Kinetics; D008054:Lipid Peroxides / Q000378:metabolism*; D008099:Liver / Q000201:enzymology*; D010084:Oxidation-Reduction; D012995:Solubility; D013552:Swine
D003902:Detergents; D007527:Isoenzymes; D008054:Lipid Peroxides; C008464:methyl linoleate hydroperoxide; D005982:Glutathione Transferase