Partial purification and characterization of a hydroxamic acid glucoside β-d-glucosidase from maize
Author
dc.contributor.author
Cuevas, Liliana
Author
dc.contributor.author
Niemeyer Marich, August
Author
dc.contributor.author
Jonsson, Lisbeth M.V.
Admission date
dc.date.accessioned
2018-12-20T14:37:57Z
Available date
dc.date.available
2018-12-20T14:37:57Z
Publication date
dc.date.issued
1992
Cita de ítem
dc.identifier.citation
Phytochemistry, Vol. 31, No. 8, pp. 2609-2612, 1992
Identifier
dc.identifier.issn
00319422
Identifier
dc.identifier.other
10.1016/0031-9422(92)83595-P
Identifier
dc.identifier.uri
https://repositorio.uchile.cl/handle/2250/156754
Abstract
dc.description.abstract
β-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