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Enzyme activity responsible for the biosynthesis of isovitexin-7-O-galactoside from isovitexin and UDP-galactose can be demonstrated in protein extracts of cotyledons and rosette leaves from Silene pratensis plants. This galactosyltransferase activity is absent in stem leaves and petals. “True Km” values of 0.0025 mᴍ for isovitexin and of 8.2 mᴍ for UDP-galactose were found. At infinite concentration of both substrates the “true V max ” value was 0.11 mᴍ/min/mg protein. The galactosyltransferase activity was optimal at pH 7.0; the divalent ions Zn and Hg were inhibitory, whereas Ca, Co, Mg, Mn and EDTA were not inhibitory.

Ontogeny and Biosynthesis of Isovitexin 7-O-Galactoside in a Mutant of Silene pratensis Unable to Glycosylate this Compound in the Petals