Occurrence of a glucosyltransferase specific for solanidine in potato plants
1991
Zimowski, J.
It was found that potato tubers, sprouts, leaves and stems show the presence of two different enzymic activities responsible for steroid glucosylation and utilization of UDPG as a donor of the glucose residue. The first is a typical UDPG: sterol glucosyltransferase bound to the membranes (105000 g pellet) which is strongly stimulated by 0.1% Triton X-100. The second enzyme is a cytosolic glucosyltransferase which is slightly inhibited by the detergent, and which shows the ability to glycosylate solanidine (22S,25S-solanid-5-en-3-beta-ol) with a high yield. The molecular weight of the latter enzyme was determined by molecular filtration on Sephadex G-150 to be ca 50000. Moreover, it was found that the cytosolic enzyme preparation also catalyses solanidine galactosylation, although with a much lower yield, using UDP-galactose as the source of the sugar residue.
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