Partial purification and characterization of a hydroxamic acid glucoside β-d-glucosidase from maize

dc.creatorCuevas, Liliana
dc.creatorNiemeyer Marich, August
dc.creatorJonsson, Lisbeth M.V.
dc.date.accessioned2018-12-20T14:37:57Z
dc.date.available2018-12-20T14:37:57Z
dc.date.created2018-12-20T14:37:57Z
dc.date.issued1992
dc.identifierPhytochemistry, Vol. 31, No. 8, pp. 2609-2612, 1992
dc.identifier00319422
dc.identifier10.1016/0031-9422(92)83595-P
dc.identifierhttp://repositorio.uchile.cl/handle/2250/156754
dc.description.abstractβ-Glucosidase activities measured in extracts from maize leaves during development gave different curves when p-nitrophenyl β-d-glucopyranoside (PNP-Glc) or hydroxamic acid glucoside (Hx-Glc) were the substrates. The PNP-Glc glucosidase had a Mr of 60 000 and an isoelectric point of 6.4, whereas the Hx-Glc glucosidase had a Mr of 158 000 and an isoelectric point of 4.8. This latter enzyme had an optimum pH of activity at 6.0, was inhibited by castanospermine and, when partially purified, accepted PNP-Glc as well as Hx-Glc as substrates, albeit with a lower activity for the former
dc.languageen
dc.publisherElsevier
dc.rightshttp://creativecommons.org/licenses/by-nc-nd/3.0/cl/
dc.rightsAttribution-NonCommercial-NoDerivs 3.0 Chile
dc.sourcePhytochemistry
dc.subjectDIMBOA.
dc.subjectGramineae
dc.subjectHydroxamic acids
dc.subjectMaize
dc.subjectZea mays
dc.subjectβ-d-glucosidase
dc.titlePartial purification and characterization of a hydroxamic acid glucoside β-d-glucosidase from maize
dc.typeArtículos de revistas


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