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  • Articles: DFG German National Licenses  (2)
  • 1980-1984  (2)
  • Albumin  (1)
  • Electro phoresis  (1)
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  • Articles: DFG German National Licenses  (2)
Material
Years
  • 1980-1984  (2)
Year
  • 1
    ISSN: 1432-2242
    Keywords: Wheat ; Endosperm ; Proteins ; Electro phoresis
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: 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.
    Type of Medium: Electronic Resource
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  • 2
    ISSN: 1432-2242
    Keywords: Phaseolus vulgaris ; Lectins ; Albumin ; Globulin
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: 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.
    Type of Medium: Electronic Resource
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