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  • 1980-1984  (2)
  • Albumin  (1)
  • Genetic variation  (1)
  • 1
    ISSN: 1432-2242
    Schlagwort(e): Phaseolus vulgaris ; Lectins ; Albumin ; Globulin
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Biologie
    Notizen: Summary Variation in the native conformation of bean lectins was examined using electrophoresis of non-denatured total protein extracts and purified albumin and globulin lectin. The observed variation was related to the genetic variation reported previously for lectin polypeptide composition as revealed by two-dimensional isoelectricfocusing-sodium dodecyl sulfate polyacrylamide gel electrophoresis (IEF-SDS/PAGE). When eleven cultivars with different IEF-SDS/PAGE lectin polypeptide compositions were compared, eight had unique non-denatured lectin patterns and three had identical patterns. For some cultivars differences in non-denatured lectin patterns were observed between the purified albumin and globulin lectin preparations.
    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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