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- W2002322605 abstract "A protein fraction migrating as a Mr 24 kDa band on SDS-PAGE was isolated by affinity chromatography on glutathione-agarose from a soluble extract of E. granulosus protoscoleces from sheep(UK). This fraction had glutathione S-transferase activity of 0.4 μmol min−1 mg−1 when measured using a standard synthetic substrate and its determined N-terminal amino acid sequence most closely resembled Mu class gluthathione S-transferases. In addition, protoscoleces from the distinct sheep and horse E. granulosus strains showed a different pattern of glutathione-binding proteins: the Mr 24 kDa species was obtained in both cases whereas an additional band of slightly faster electrophoretic mobility was isolated from horse(UK) protoscoleces." @default.
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- W2002322605 title "Isolation and biochemical characterisation of a glutathione S-transferase from Echiococcus granulosus protoscoleces" @default.
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- W2002322605 doi "https://doi.org/10.1016/0020-7519(94)90172-4" @default.
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