Thidarat EksittikulMontri ChulavatnatolMahidol University2018-06-142018-06-141988-01-01Archives of Biochemistry and Biophysics. Vol.266, No.1 (1988), 263-26910960384000398612-s2.0-0024095252https://repository.li.mahidol.ac.th/handle/20.500.14594/15498Linamarase (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.Mahidol UniversityBiochemistry, Genetics and Molecular BiologyArticleSCOPUS10.1016/0003-9861(88)90257-3