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Note | Special issue | Vol 56, No. 1-2, 2002, pp.509-514
Published online, 1st January, 1970
DOI: 10.3987/COM-01-S(K)28
Isolation and Characterization of UDP-glucosyltransferase in the Cultured Cells of Nicotiana tabacum

Shin-ya Yamane, Kei Shimoda, Takeshi Fujino, Shinji Ohta, and Toshifumi Hirata*

*Department of Mathematical and Life Sciences, Graduate School of Science, Hiroshima University, 1-3-1 Kagamiyama, Higashi-hiroshima, Hiroshima 739-8526, Japan


A glucosyltransferase, catalyzing the transfer of glucose from UDP-glucose to hydroxycoumarins, was isolated from the cultured cells of Nicotiana tabacum. The glucosyltransferase was purified to electrophoretic homogeneity by a procedure involving Sephadex G-25, Agarose-gel affinity, and Sephadex G-200 columns; the enzyme has molecular mass of 61 kDa and pH optimum at 8.0 and the activity was inhibited by divalent metal ions such as Co2+ and Zn2+. The enzyme glucosylated preferentially 7-hydroxyl group of hydroxycoumarins.