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dc.contributor.authorRodjana Opassirien_US
dc.contributor.authorJames R. Ketudat Cairnsen_US
dc.contributor.authorTakashi Akiyamaen_US
dc.contributor.authorOnnop Wara-Aswapatien_US
dc.contributor.authorJisnuson Svastien_US
dc.contributor.authorAsim Esenen_US
dc.contributor.otherSuranaree University of Technologyen_US
dc.contributor.otherHokkaido Agricultural Research Center, NAROen_US
dc.contributor.otherMahidol Universityen_US
dc.contributor.otherVirginia Polytechnic Institute and State Universityen_US
dc.date.accessioned2018-07-24T03:17:19Z-
dc.date.available2018-07-24T03:17:19Z-
dc.date.issued2003-09-01en_US
dc.identifier.citationPlant Science. Vol.165, No.3 (2003), 627-638en_US
dc.identifier.issn01689452en_US
dc.identifier.other2-s2.0-0042130165en_US
dc.identifier.urihttps://www.scopus.com/inward/record.uri?partnerID=HzOxMe3b&scp=0042130165&origin=inwarden_US
dc.identifier.urihttp://repository.li.mahidol.ac.th/dspace/handle/123456789/20622-
dc.description.abstractThe cDNAs for two β-glucosidase (E.C. 3.2.1.21) isozymes from rice (Oryza sativa L.), designated bglu1 and bglu2, were cloned and sequenced. The cDNA sequences for bglu1 and bglu2 included open reading frames encoding 504 and 500 amino acid precursor proteins, respectively. Both of these enzymes appeared to enter the secretory pathway, as judged by their N-terminal signal sequences. Southern blots using gene-specific probes indicated that bglu1 and bglu2 were single copy genes. The bglu1 and bglu2 mRNAs were highly expressed in the shoot during germination, with a similar time course. However, differences were seen in expression in mature plants, where bglu1 was highly expressed in flowers, but bglu2 was not. A recombinant thioredoxin fusion protein produced from the bglu1 cDNA in redox-deficient Excherichia coli (BGlu1) hydrolyzed p-nitrophenol β-D-glucoside, β-D-fucoside, and other p-nitrophenol β-D-glycosides, and was strongly inhibited by glucono-1,5-lactone. It also hydrolyzed some natural glucosides, including the rice-derived pyridoxine-5′-O-β-D-glucoside, and hydrolyzed and transglycosylated short β-(1 → 3) and β-(1 → 4) linked gluco-oligosaccharides. Based on the results, possible functions of BGlu1 include hydrolysis and recycling of oligosaccharides generated from rapid cell wall expansion during seed germination and flower expansion, and release of the coenzyme pyridoxine from its glucose-conjugated storage form. © 2003 Elsevier Ireland Ltd. All rights reserved.en_US
dc.rightsMahidol Universityen_US
dc.source.urihttps://www.scopus.com/inward/record.uri?partnerID=HzOxMe3b&scp=0042130165&origin=inwarden_US
dc.subjectAgricultural and Biological Sciencesen_US
dc.subjectBiochemistry, Genetics and Molecular Biologyen_US
dc.titleCharacterization of a rice β-glucosidase highly expressed in flower and germinating shooten_US
dc.typeArticleen_US
dc.rights.holderSCOPUSen_US
dc.identifier.doi10.1016/S0168-9452(03)00235-8en_US
Appears in Collections:Scopus 2001-2005

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