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Blocking factors and the isolation of glutathione transferases from Hymenolepis diminuta (Cestoda: Cyclophyllidea)

Published online by Cambridge University Press:  06 April 2009

P. M. Brophy
Affiliation:
Department of Biological Sciences, University College of Wales, Aberystwyth, Dyfed SY23 3DA, UK
J. Barrett
Affiliation:
Department of Biological Sciences, University College of Wales, Aberystwyth, Dyfed SY23 3DA, UK

Summary

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.

Type
Research Article
Copyright
Copyright © Cambridge University Press 1990

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