Isolation and biochemical characterisation of a glutathione S-transferase from Echinococcus granulosus protoscoleces.
A protein fraction migrating as a M(r) 24 kDa band on SDS-PAGE was isolated by affinity chromatography on glutathione-agarose from a soluble extract of E. granulosus proto-scoleces from sheep(UK). This fraction had glutathione S-transferase activity of 0.4 mumol min-1 mg-1 when measured using a standard synthetic substrate and its determined N-terminal amino acid sequence most closely resembled Mu class glutathione S-transferases. In addition, protoscoleces from the distinct sheep and horse E. granulosus strains showed a different pattern of glutathione-binding proteins: the M(r) 24 kDa species was obtained in both cases whereas an additional band of slightly faster electrophoretic mobility was isolated from horse(UK) protoscoleces.
Fernández
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Department of Pathology, University of Cambridge, U.K.
Hormaeche
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CE
D000595:Amino Acid Sequence; D000818:Animals; D015153:Blotting, Western; D004446:Echinococcus / Q000201:enzymology*; D005982:Glutathione Transferase / Q000737:chemistry / Q000276:immunology / Q000302:isolation & purification*; D008969:Molecular Sequence Data; D017421:Sequence Analysis; D017386:Sequence Homology, Amino Acid
D005982:Glutathione Transferase