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Characterization of cyanogenic β-glucosidase (Linamarase) from cassava (Manihot esculenta Crantz)

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dc.contributor.authorThidarat Eksittikulen_US
dc.contributor.authorMontri Chulavatnatolen_US
dc.contributor.otherMahidol Universityen_US
dc.date.accessioned2018-06-14T09:06:26Z
dc.date.available2018-06-14T09:06:26Z
dc.date.issued1988-01-01en_US
dc.description.abstractLinamarase (EC 3.2.1.21) was purified from cassava petiole, stem, and root cortex by ammonium sulfate precipitation, column chromatography on Sepharose 6B, and chromatofocusing. The last step resolved the enzyme from each source into three forms with pI values of 4.3, 3.3, and 2.9. Each form was found to be oligomeric, consisting of one kind of subunit, M r 63,000. The major isozyme with a pI of 4.3 from petiole showed a K m for linamarin of 0.6 mm and possessed both β-glucosidase and β-fucosidase activities. The former was sensitive to inhibition by δ-gluconolactone, isopropyl-β-d-thioglucoside, and HgCl 2 , whereas the latter was inhibited by Tris ion. © 1988.en_US
dc.identifier.citationArchives of Biochemistry and Biophysics. Vol.266, No.1 (1988), 263-269en_US
dc.identifier.doi10.1016/0003-9861(88)90257-3en_US
dc.identifier.issn10960384en_US
dc.identifier.issn00039861en_US
dc.identifier.other2-s2.0-0024095252en_US
dc.identifier.urihttps://repository.li.mahidol.ac.th/handle/20.500.14594/15498
dc.rightsMahidol Universityen_US
dc.rights.holderSCOPUSen_US
dc.source.urihttps://www.scopus.com/inward/record.uri?partnerID=HzOxMe3b&scp=0024095252&origin=inwarden_US
dc.subjectBiochemistry, Genetics and Molecular Biologyen_US
dc.titleCharacterization of cyanogenic β-glucosidase (Linamarase) from cassava (Manihot esculenta Crantz)en_US
dc.typeArticleen_US
dspace.entity.typePublication
mu.datasource.scopushttps://www.scopus.com/inward/record.uri?partnerID=HzOxMe3b&scp=0024095252&origin=inwarden_US

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