Purification and properties of glutathione S-transferase from outer mitochondrial membrane of rat liver.
Glutathione S-transferase located in outer mitochondrial membrane was purified from rat liver into homogeneous state on SDS-PAGE by two steps of chromatography. Outer mitochondrial membrane glutathione S-transferase was immunochemically related with microsomal glutathione S-transferase and shared similar characteristics each other, e.g., stimulation of the activity by treatment with N-ethylmaleimide, molecular weight, optimal pH, substrate specificities, glutathione peroxidase activity, kinetic parameters, amino acid composition and profile of peptide mapping by protease.
Nishino
H
H
Department of Biology, Faculty of Science, Kyushu University, Fukuoka, Japan.
Ito
A
A
D000596:Amino Acids / Q000032:analysis; D000818:Animals; D002845:Chromatography; D005982:Glutathione Transferase / Q000302:isolation & purification / Q000378:metabolism*; D006863:Hydrogen-Ion Concentration; D015151:Immunoblotting; D007425:Intracellular Membranes / Q000201:enzymology; D007700:Kinetics; D008297:Male; D008930:Mitochondria, Liver / Q000201:enzymology*; D010449:Peptide Mapping; D051381:Rats; D011919:Rats, Inbred Strains; D013379:Substrate Specificity
D000596:Amino Acids; D005982:Glutathione Transferase