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  • 1980-1984  (2)
  • Banding types  (1)
  • Endosperm  (1)
  • 1
    ISSN: 1432-2242
    Schlagwort(e): Wheat ; Endosperm ; Proteins ; Electro phoresis
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Biologie
    Notizen: Summary The major endosperm proteins in a range of genotypes of hexaploid wheat have been fractionated by two-dimensional electrophoresis. The genotypes included nine varieties and forty four intervarietal substitution lines in which chromosomes 1A, 1B, 1D, 6A, 6B or 6D from eight of the varieties have been introduced one at a time into a common genetic background. The appearance of different protein subunits was often correlated with a chromosome substitution. This showed that many of the genes for the high molecular weight protein subunits (molecular weight range 55,000 to 140,000 determined by SDS polyacrylamide gel electrophoresis) are specified by chromosomes 1A, 1B and 1D while many of the lower molecular weight subunits (molecular weight range 30,000 to 45,000) are specified by chromosomes 6A, 6B and 6D. The different protein subunits correlated with chromosome substitution could not always be recognised in the varietal source of the substituted chromosome. The different subunits specified by homologous chromosomes in different wheat varieties may differ in isoelectric point and/or molecular weight.
    Materialart: Digitale Medien
    Bibliothek Standort Signatur Band/Heft/Jahr Verfügbarkeit
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  • 2
    Digitale Medien
    Digitale Medien
    Springer
    Theoretical and applied genetics 59 (1981), S. 83-88 
    ISSN: 1432-2242
    Schlagwort(e): Phaseolus vulgaris ; Storage proteins ; Electrophoresis ; Genetic variation ; Banding types
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Biologie
    Notizen: Summary Charge and molecular weight heterogeneity of globulin-1 (G1) polypeptides of the bean, Phaseolus vulgaris L., were revealed by sodium dodecyl sulphate-polyacrylamide gel electrophoresis (SDS-PAGE). Different bean cultivars were classified into three groups: ‘Tendergreen’, ‘Sanilac’, and ‘Contender’ on the basis of their protein subunit composition. Nine distinct major bands: α51,α49, α48.5,β48T, β48S, β47, γ45.5, γ45S, and γ45C, and two minor bands: γ46T and γ46S were found to account for the three profiles seen on one-dimensional SDS-PAGE. Two-dimensional analysis revealed these eleven protein bands to be composed of a minimum of fourteen distinct protein subunits. The ‘Tendergreen’ and ‘Sanilac’ types differ in their G1 polypeptide composition. The protein patterns of the ‘Contender’ types are intermediate, containing many protein subunits found in the patterns of the ‘Tendergreen’ and ‘Sanilac’ types suggesting a genetic and evolutionary relationship.
    Materialart: Digitale Medien
    Bibliothek Standort Signatur Band/Heft/Jahr Verfügbarkeit
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