Detoxification reactions of Fasciola hepatica cytosolic glutathione transferases.
Acidic/neutral glutathione (GSH) transferase forms have been isolated from Fasciola hepatica by a combination of GSH-affinity chromatography and chromatofocusing. Approximately 10-25% of the activity failed to interact with the GSH-affinity matrix when applied from crude cytosolic preparations. Following partial purification by chromatofocusing this GSH transferase activity did subsequently bind to the affinity matrix. The F. hepatica GSH transferases had catalytic activity with secondary lipid peroxidation products, the latter being possible natural substrates. The enzymes also interacted with a number of hydrophobic ligands including haematin and substituted phenol-based anthelmintics.
Brophy
P M
PM
Department of Biological Sciences, University College of Wales, Aberystwyth, Dyfed, U.K.
Crowley
P
P
Barrett
J
J
D000818:Animals; D000871:Anthelmintics / Q000378:metabolism; D002846:Chromatography, Affinity; D003600:Cytosol / Q000201:enzymology*; D005210:Fasciola hepatica / Q000201:enzymology*; D005982:Glutathione Transferase / Q000037:antagonists & inhibitors / Q000302:isolation & purification / Q000378:metabolism*; D006863:Hydrogen-Ion Concentration; D007525:Isoelectric Focusing; D015227:Lipid Peroxidation; D013379:Substrate Specificity
D000871:Anthelmintics; D005982:Glutathione Transferase