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  • 2000-2004
  • 1980-1984  (2)
  • Agglutination  (1)
  • Endosperm  (1)
  • 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
    Electronic Resource
    Electronic Resource
    Springer
    Theoretical and applied genetics 62 (1982), S. 263-271 
    ISSN: 1432-2242
    Keywords: Phaseolus vulgaris ; Seed protein ; Lectins ; Electrophoresis ; Agglutination
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary Single seeds of over 100 bean cultivars were analyzed by two-dimensional electrophoresis. The cultivars could be classified into eight groups by virtue of their G2/albumin electrophoretic patterns: TG2, SG2, VG2, PrG2, BG2, MG2, PG2, and PiG2, The polypeptide compositions of these types were largely inter-related having particular polypeptides in common. It was possible to correlate the G2/albumin patterns with agglutinating activity of cow and rabbit blood cells as measured by the agglutination ratio (minimum concentration of extract required to agglutinate cow blood cells: minimum concentration of extract required to agglutinate rabbit blood cells). The active lectin polypeptides were identified by extracting lectins from agglutinated erythrocytes and by comparing the qualitative similarities and differences of the G2/albumin patterns and their agglutination activities. A reference catalogue of over 100 bean cultivars giving their phaseolin and G2/albumin electrophoretic patterns, and agglutination ratios is presented.
    Type of Medium: Electronic Resource
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