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'Anthocyanins' in keywords Facet   Publication Year 1980  [X]
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1980[X]
1Author    D. Ieter, S. Track3, N. Aam, A. Kaviab, HansR. EznikaRequires cookie*
 Title    High Performance Liquid Chromatographic Identification of Anthocyanins  
 Abstract    A high performance liquid chromatographic procedure for a rapid identification o f antho­ cyanins is described. Besides their characteristic retention times, anthocyanins can easily be identified by an HPLC examination o f the kinetics of appearance and disappearance o f their partial hydrolysis products. This method is also applicable to 3-deoxyanthocyanins which is demonstrated with an extract from the fern Blechnum brasiliense. The described method allows optimal resolution of complex anthocyanin mixtures in the fol­ lowing sequence o f elution: 3-sophoroside-5-glucoside; 3-rutinoside-5-glucoside; 3,5-diglucoside; 3-sophoroside; 3-galactoside; 3-glucoside; 3-rutinoside; 5-glucoside; aglycone, and finally the forms acylated with /?-coumaric acid. Substitution in the B-ring o f the aglycone structure is the key factor for the range o f the retention time. Thus cyanidin 3,5-diglucoside elutes earlier (—38 sec) than pelargonidin 3-sophoroside-5-glucoside. 
  Reference    Z. Naturforsch. 35c, 533—538 (1980); received March 20 1980 
  Published    1980 
  Keywords    Anthocyanins, 3-Deoxyanthocyanins, Partial Hydrolysis, High Performance Liquid Chromato­ graphy 
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 TEI-XML for    default:Reihe_C/35/ZNC-1980-35c-0533.pdf 
 Identifier    ZNC-1980-35c-0533 
 Volume    35 
2Author    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