Blocking factors and the isolation of glutathione transferases from Hymenolepis diminuta (Cestoda: Cyclophyllidea).
Four acidic glutathione (GSH) transferase forms were isolated from the cytosol of the adult cestode Hymenolepis diminuta by hydroxylapatite chromatography, glutathione-affinity chromatography and chromatofocusing, pH 7-5. The enzymes were dimers of subunit size approximately 24 kDa and accounted for at least 3% of the total soluble protein. The major GSH transferase had limited catalytic activity but may interact with a range of ligands and function as a binding/passive detoxification protein. An endogenous factor interfered with the binding of the crude cytosolic GSH transferase activity to glutathione-dependent affinity matrices but, following partial purification, the GSH transferase activity successfully interacted with the glutathione affinity matrix.
Brophy
P M
PM
Department of Biological Sciences, University College of Wales, Aberystwyth, Dyfed, UK.
Barrett
J
J
D000818:Animals; D001667:Binding, Competitive; D002846:Chromatography, Affinity; D002850:Chromatography, Gel; D004591:Electrophoresis, Polyacrylamide Gel; D005982:Glutathione Transferase / Q000032:analysis / Q000302:isolation & purification*; D006926:Hymenolepis / Q000201:enzymology*; D007525:Isoelectric Focusing; D008024:Ligands; D013379:Substrate Specificity
D008024:Ligands; D005982:Glutathione Transferase