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Showing papers on "Isovitexin published in 1975"


Journal ArticleDOI
TL;DR: Isoorientin, isovitex in, isoorientin-4′-O-glucoside and isovITExin- 4′- O-glUCoside have been identified in the leaves and roots of Gentiana punctata L., and in the Leaves of G. purpurea L., G. pannonica Scop, G. villarsii Ronn.

20 citations


Journal ArticleDOI
TL;DR: In the growing shoot of oat seedlings generally four C-glycosylflavones are synthesized generally and accumulate to 97–99 % in the primary leaf, which is found in all developmental stages, independent of light.

18 citations


Journal ArticleDOI
TL;DR: The results support the suggestion that PAL- or TAL-reactions are not rate limiting in the biosynthesis of Avena-glycosylflavones, but that enzymes catalyzing subsequent reactions, mainly C15-enzymes including CFI, control the rate of flavone synthesis.

12 citations


Journal ArticleDOI
TL;DR: A competition model is proposed which explains why the amounts of isovitexin 7-0-xyloside in gXgX and isovITExin7-0 -glucosideIn gGgG plants are about the same, whereas in gGGX plants isovitesvitex in 7- 0-xoloside escapes dejection.
Abstract: In the petals of Melandrium the glycosylation of the 7-hydroxylgroup of isovitexin is governed by a series of 4 multiple alleles: gG, g, gX, and $${\text{g}}^{{\text{X}}^{\text{1}} }$$ Gene gG is the structural gene for UDP-glucose: isovitexin 7-0-glucosyltransferase; the alleles gX and $${\text{g}}^{{\text{X}}^{\text{1}} }$$ are structural genes for UDP-xylose: isovitexin 7-0-xylosyltransferase Gene g is inactive and does not produce a functional glycosyltransferase In the presence of both gene gG and its allele gX the product of gene gX (isovitexin 7-0-xyloside) is not detectable In this respect gene gG is dominant over its allele gX In petal extracts of these gG/gX plants, xylosyltransferase, as well as glucosyltransferase, can be detected The dominance is therefore not a consequence of transcriptional and/or translational control Enzyme kinetic experiments demonstrated that inhibition of xylosyltransferase by the end product of glucosyltransferase did not occur Comparison of the enzyme kinetic parameters revealed that dominance is probably caused by differences in Vmax between the two enzymes, both working at saturating isovitexin concentrations A competition model is proposed which explains why the amounts of isovitexin 7-0-xyloside in gXgX and isovitexin 7-0-glucoside in gGgG plants are about the same, whereas in gGgX plants isovitexin 7-0-xyloside escapes dejection This competition model is supported by the enzyme kinetic results found with the codominant allele $${\text{g}}^{{\text{X}}^{\text{1}} }$$

9 citations