The purification and properties of glutathione S-transferase from Ditylenchus myceliophagus
Summary- The cytoplasmic glutathione S-transferase (GST) activity of Ditylenchus myceliophagus was resolved intO four isoforms, DmI, DmII, DmIII and DmIV, by a combination of chromatofocusing and hexylglutathione affinity chromatOgraphy. An endogenous cytoplasmic factOr interfered with the binding o...
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ftciteseerx:oai:CiteSeerX.psu:10.1.1.584.298 2023-05-15T16:02:04+02:00 The purification and properties of glutathione S-transferase from Ditylenchus myceliophagus Anna D. Persauo N. Perry John Barrett The Pennsylvania State University CiteSeerX Archives application/pdf http://citeseerx.ist.psu.edu/viewdoc/summary?doi=10.1.1.584.298 http://horizon.documentation.ird.fr/exl-doc/pleins_textes/fan/010011813.pdf en eng http://citeseerx.ist.psu.edu/viewdoc/summary?doi=10.1.1.584.298 http://horizon.documentation.ird.fr/exl-doc/pleins_textes/fan/010011813.pdf Metadata may be used without restrictions as long as the oai identifier remains attached to it. http://horizon.documentation.ird.fr/exl-doc/pleins_textes/fan/010011813.pdf text ftciteseerx 2016-08-28T00:06:16Z Summary- The cytoplasmic glutathione S-transferase (GST) activity of Ditylenchus myceliophagus was resolved intO four isoforms, DmI, DmII, DmIII and DmIV, by a combination of chromatofocusing and hexylglutathione affinity chromatOgraphy. An endogenous cytoplasmic factOr interfered with the binding of the cytosolic transferases to glutathione and hexylglutathione affmity matrices and binding only occurred after initial purification. The four isoforms were homodimers with subunit mole-cular weights 25.3, 24, 26 and 25.7 kDa for DmI, II, III and IV, respectively. The pIs for DmI, II and III were 7.28, 5.04 and 4.88. The N-terminal sequence of the major form (DmIII) had a strong sequence similarity to the mammalian alpha class GSTs. However, substrate specificities and inhibitor profiles of Dm II, III and IV showed an overall resemblance to the mammalian mu class, whilsr DmI showed more alpha class characteristics. Résumé- Purification et propriétés de la glutathion S-transférase isolée de Ditylenchus myceliophagus- L'activité de la glutathion S-transférase cytoplasmique chez Ditytenchus myceliophagus a été attribuée à quatre isoenzymes, Dml, DmII, DmlII et DmIV, par combinaison de la chromatographie focalisante et de la chromatographie d'affinité au moyen de l'hexyl-glutathion. Un facteur endogéne cytoplasmique a interféré avec les matrices d'affinité de la liaison entre les transférases cyto-soliques et le glutathion, et la liaison ne s'est produite qu'après une purification prèliminaire. Les quatres isoenzymes sont apparues être des homodimères avec des subunitès de poids moléculaires respectifs de 25,3, 24, 26 et 25,7 kDa pour DllÙ, DmII, DmIli et DmIY. Les points isoélecrriques pour DmI, DmII et DmIII sont de 7,28, 5,04 et 4,88. La séquence N-termi- Text DML Unknown |
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Summary- The cytoplasmic glutathione S-transferase (GST) activity of Ditylenchus myceliophagus was resolved intO four isoforms, DmI, DmII, DmIII and DmIV, by a combination of chromatofocusing and hexylglutathione affinity chromatOgraphy. An endogenous cytoplasmic factOr interfered with the binding of the cytosolic transferases to glutathione and hexylglutathione affmity matrices and binding only occurred after initial purification. The four isoforms were homodimers with subunit mole-cular weights 25.3, 24, 26 and 25.7 kDa for DmI, II, III and IV, respectively. The pIs for DmI, II and III were 7.28, 5.04 and 4.88. The N-terminal sequence of the major form (DmIII) had a strong sequence similarity to the mammalian alpha class GSTs. However, substrate specificities and inhibitor profiles of Dm II, III and IV showed an overall resemblance to the mammalian mu class, whilsr DmI showed more alpha class characteristics. Résumé- Purification et propriétés de la glutathion S-transférase isolée de Ditylenchus myceliophagus- L'activité de la glutathion S-transférase cytoplasmique chez Ditytenchus myceliophagus a été attribuée à quatre isoenzymes, Dml, DmII, DmlII et DmIV, par combinaison de la chromatographie focalisante et de la chromatographie d'affinité au moyen de l'hexyl-glutathion. Un facteur endogéne cytoplasmique a interféré avec les matrices d'affinité de la liaison entre les transférases cyto-soliques et le glutathion, et la liaison ne s'est produite qu'après une purification prèliminaire. Les quatres isoenzymes sont apparues être des homodimères avec des subunitès de poids moléculaires respectifs de 25,3, 24, 26 et 25,7 kDa pour DllÙ, DmII, DmIli et DmIY. Les points isoélecrriques pour DmI, DmII et DmIII sont de 7,28, 5,04 et 4,88. La séquence N-termi- |
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The Pennsylvania State University CiteSeerX Archives |
format |
Text |
author |
Anna D. Persauo N. Perry John Barrett |
spellingShingle |
Anna D. Persauo N. Perry John Barrett The purification and properties of glutathione S-transferase from Ditylenchus myceliophagus |
author_facet |
Anna D. Persauo N. Perry John Barrett |
author_sort |
Anna D. Persauo |
title |
The purification and properties of glutathione S-transferase from Ditylenchus myceliophagus |
title_short |
The purification and properties of glutathione S-transferase from Ditylenchus myceliophagus |
title_full |
The purification and properties of glutathione S-transferase from Ditylenchus myceliophagus |
title_fullStr |
The purification and properties of glutathione S-transferase from Ditylenchus myceliophagus |
title_full_unstemmed |
The purification and properties of glutathione S-transferase from Ditylenchus myceliophagus |
title_sort |
purification and properties of glutathione s-transferase from ditylenchus myceliophagus |
url |
http://citeseerx.ist.psu.edu/viewdoc/summary?doi=10.1.1.584.298 http://horizon.documentation.ird.fr/exl-doc/pleins_textes/fan/010011813.pdf |
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http://horizon.documentation.ird.fr/exl-doc/pleins_textes/fan/010011813.pdf |
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http://citeseerx.ist.psu.edu/viewdoc/summary?doi=10.1.1.584.298 http://horizon.documentation.ird.fr/exl-doc/pleins_textes/fan/010011813.pdf |
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