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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  and
J. Barrett
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
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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.

Keywords

Hymenolepis diminutaglutathione transferasecestodelipid peroxidationanthelminticbinding protein
Type
Research Article
Information
Parasitology , Volume 100 , Issue 1 , February 1990 , pp. 137 - 141
Copyright
Copyright © Cambridge University Press 1990

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