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Purification and biochemical characterization of cytosolic glutathione-S-transferase from filarial worms Setaria cervi.
Ahmad, Rumana; Srivastava, Arvind K; Walter, Rolf D.
Afiliação
  • Ahmad R; Division of Biochemistry, P.O. Box No. 173, Central Drug Research Institute, Chattar Manzil Palace, Lucknow-226001, India.
Comp Biochem Physiol B Biochem Mol Biol ; 151(3): 237-45, 2008 Nov.
Article em En | MEDLINE | ID: mdl-18752976
ABSTRACT
The present study reports the purification and characterization of GST from cytosolic fraction of Setaria cervi. GST activity was determined in various subcellular fractions of bovine filarial worms S. cervi (Bubalus bubalis Linn.) and was found to be localized mainly in the cytosolic and microsomal fractions. The soluble enzyme from S. cervi was purified to homogeneity using a combination of salt precipitation, centrifugation, cation exchange and GSH-Sepharose affinity chromatography followed by ultrafiltration. SDS-PAGE analysis revealed a single band and activity staining was also detected on PAGE gels. Gel filtration and MALDI-TOF studies revealed that the native enzyme is a homodimer with a subunit molecular mass of 24.6 kDa. Comparison of kinetic properties of the parasitic and mammalian enzymes revealed significant differences between them. The substrate specificity and inhibitor profile of cytosolic GST from S. cervi appeared to be different from GST from mammalian sources.
Assuntos

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Setaria (Nematoide) / Glutationa Transferase Limite: Animals Idioma: En Ano de publicação: 2008 Tipo de documento: Article

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Setaria (Nematoide) / Glutationa Transferase Limite: Animals Idioma: En Ano de publicação: 2008 Tipo de documento: Article