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'Matthiola incana' in keywords
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1984 (1)
1983 (1)
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1980 (1)
1Author    R. R. Br, G. Spribille, ForkmRequires cookie*
 Title    Genetic Control of Chalcone Synthase Activity in Flowers of Matthiola incana  
 Abstract    Chalcone synthase activity was demonstrated in enzyme preparations from flowers o f defined genotypes of Matthiola incana (stock). The product formed from 4-coumaroyl-CoA and malonyl-CoA was naringenin and not the isomeric chalcone, because chalcone isomerase was also present in the reaction mixture. Chalcone synthase activity could be detected only in flower extracts o f genotypes with wild-type alleles at the locus f Thus, the interruption of the anthocyanin pathway in white flowering lines with recessive alleles (ff) of this gene is clearly due to a lack o f this enzyme activity. Independent on the genetic state of the locus b which controls the formation of pelargonidin or cyanidin, respectively, in the flowers, 4-coumaroyl-CoA was the only suitable substrate for the condensation reaction. 
  Reference    Z. Naturforsch. 36c, 619 (1981); received April 3 1981 
  Published    1981 
  Keywords    Anthocyanins, Flavonoids, Chalcone Synthase, Genetic Control, Matthiola incana 
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 TEI-XML for    default:Reihe_C/36/ZNC-1981-36c-0619.pdf 
 Identifier    ZNC-1981-36c-0619 
 Volume    36 
2Author    V. HemlebenRequires cookie*
 Title    Anthocyanin Carrying Structures in Specific Genotypes of Matthiola incana R. Br  
 Abstract    Several lines of the genetically well defined Matthiola incana (Brassicaceae) concerning the anthocyanin biosynthesis (line 02, 06, 10, and 14) store the anthocyanin pigment as crystals (line 06) or in anthocyanoblasts ("balls") in the epidermal cells (line 02, 10, and 14) o f the flower petals. The genetic constitution o f these genotypes is in addition to the basic factors f +, g+, and e+, b+b+ or bb (cyanidin or pelargonidin type), 11, u+u+, and v+v+ or vv, demonstrating that the 11, u+u+ constitution is responsible for precipitation of anthocyanins in a certain structure indepen­ dent of the other modificationally acting genes b and v. The 11, u+u+ types accumulate preferentially acylated 3-biosides. 
  Reference    Z. Naturforsch. 36c, 925 (1981); received September 29 1981 
  Published    1981 
  Keywords    Anthocyanin, 3-Biosides, Crystals, Matthiola incana, Brassicaceae 
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 TEI-XML for    default:Reihe_C/36/ZNC-1981-36c-0925.pdf 
 Identifier    ZNC-1981-36c-0925 
 Volume    36 
3Author    R. R. Br, G. Spribille, ForkmannRequires cookie*
 Title    Conversion of Dihydroflavonols to Flavonols with Enzyme Extracts from Flower Buds of Matthiola incana  
 Abstract    Soluble enzyme preparations from flower buds of Matthiola incana catalysed the conversion of dihydrokaempferol to kaempferol and of dihydroquercetin to quercetin. The reaction required 2-oxoglutarate, ascorbate and Fe2+ as cofactors and had a pH-optimum at about 7.0. Highest enzyme activity was already present in the youngest buds followed by a rapid decline during bud and flower development. Furthermore, a substantial correlation was observed between the enzyme activity for flavonol formation and the flavonol content of the buds and flowers. 
  Reference    Z. Naturforsch. 39c, 714—719 (1984); received April 4/May 23 1984 
  Published    1984 
  Keywords    Dioxygenase, Flavonoid Biosynthesis, Flavonols, Matthiola incana 
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 TEI-XML for    default:Reihe_C/39/ZNC-1984-39c-0714.pdf 
 Identifier    ZNC-1984-39c-0714 
 Volume    39 
4Author    G. Forkm, W. Heller, H. GrisebachRequires cookie*
 Title    Anthocyanin Biosynthesis in Flowers of Matthiola incana Flavanone 3-and Flavonoid 3'-Hydroxylases  
 Abstract    Enzyme preparations from flowers o f defined genotypes o f Matthiola incana contain two dif­ ferent hydroxylases for hydroxylation of naringenin in the 3-and 3'-position, respectively. The 3-hydroxylase is a soluble enzyme and requires as cofactors 2-oxoglutarate, Fe2+ and ascorbate. Besides naringenin eriodictyol is a substrate for the 3-hydroxylase. The 3'-hydroxylase is localized in the microsomal fraction and requires NADPH as cofactor. Naringenin and dihydro-kaempferol but not 4-coumarate or 4-coumaroyl-CoA are substrates for this enzyme. 3'-Hy-droxylase activity is present only in genetic lines of M. incana with the wild-type allele b +. 
  Reference    Z. Naturforsch. 35c, 691—6 (1980); received June 25 1980 
  Published    1980 
  Keywords    Anthocyanins, Flavonoids, Biosynthesis, Flavanon 3-Hydroxylase, Flavonoid 3'-Hydroxylase, Matthiola incana 
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 TEI-XML for    default:Reihe_C/35/ZNC-1980-35c-0691.pdf 
 Identifier    ZNC-1980-35c-0691 
 Volume    35 
5Author    B. D. Angelm Ayr, G. Stotz, R. Spribille, O. RkRequires cookie*
 Title    Relationship between Flower Development, Anthocyanin Accumulation and Activity o f Enzymes Involved in Flavonoid Biosynthesis in Matthiola incana R. Br  
 Abstract    The activity of five enzymes concerning anthocyanin biosynthesis as well as the anthocyanin accumulation were studied during the developm ent o f buds and flowers o f Matthiola incana. The investigations included the first three enzymes in the anthocyanin pathw ay, chalcone synthase, chalcone isomerase and flavanone 3-hydroxylase, and the flavonoid-m odifying enzymes, flavo-noid 3'-hydroxylase and flavonoid 3-O-glucosyltransferase. The bud and flower development was subdivided into eight stages with respect to m orphological criteria. On a fresh weight basis, a substantial correlation between anthocyanin content and the activities o f all o f the five enzymes were found in the various developmental stages. Furtherm ore, the anthocyanins formed are obviously not or only less subject to degradation. Although all m axim a of activity proved to be in buds, clear differences were observed between the five enzymes with regard to increase and stage of maximum activity. The isolation of other enzymes involved in flavonoid biosynthesis is likely to be most successful in the bud stages. 
  Reference    Z. Naturforsch. 38c, 551—555 (1983); received April 111983 
  Published    1983 
  Keywords    Matthiola incana, Anthocyanin Biosynthesis, Anthocyanin Content, Enzyme Activities, Flower Development 
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 TEI-XML for    default:Reihe_C/38/ZNC-1983-38c-0551.pdf 
 Identifier    ZNC-1983-38c-0551 
 Volume    38