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  • 1980-1984  (2)
  • 1950-1954
  • Banding types  (1)
  • Glutenin  (1)
  • 1
    Electronic Resource
    Electronic Resource
    Genetic variation in the subunits of globulin-1 storage protein of French bean (1981)
    Springer
    Theoretical and applied genetics 59 (1981), S. 83-88 
    Details
    ISSN: 1432-2242
    Keywords: Phaseolus vulgaris ; Storage proteins ; Electrophoresis ; Genetic variation ; Banding types
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: 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.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00285895
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Fractionation of wheat gliadin and glutenin subunits by two-dimensional electrophoresis and the role of group 6 and group 2 chromosomes in gliadin synthesis (1981)
    Springer
    Theoretical and applied genetics 59 (1981), S. 349-359 
    Details
    ISSN: 1432-2242
    Keywords: Triticum aestivum ; Glutenin ; Gliadin ; Electrophoresis
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary Subunits of wheat endosperm proteins have been fractionated by two-dimensional electrophoresis. To determine which subunits in the two-dimensional electrophoretic pattern belong to gliadin or glutenin the endosperm proteins have also been fractionated by a modified Osborne procedure and by gel filtration on Sephadex G-100 and Sepharose CL-4B prior to separation by two-dimensional electrophoresis. The control of production of five major grain protein subunits is shown to be determined by chromosomes 6A, 6B and 6D by comparing two-dimensional electrophoretic protein subunit patterns of aneuploid lines of the variety ‘Chinese Spring’. From these and previous studies it is concluded that some α, β and γ gliadins (molecular weights by SDS-PAGE 30,000 to 40,000) are specified by genes on the short arms of homoeologous Group 6 chromosomes, the ω gliadins (molecular weights by SDS-PAGE 50,000 to 70,000) are specified by genes on the short arms of homoeologous Group 1 chromosomes and the glutenin subunits (molecular weights by SDS-PAGE 〉 85,000) are specified by genes on the long arms of homoeologous Group 1 chromosomes. No major gliadins or glutenin subunits were absent when any of the chromosomes in homoeologous Groups 2, 3, 4, 5 or 7 were deleted. However two gliadins whose presumed structural genes are on chromosome 6D were absent in aneuploid stocks of ‘Chinese Spring’ carrying two additional doses of chromosome 2A. Two out of thirty-three intervarietal or interspecific chromosome substitution lines examined, involving homoeologous Group 2 chromosomes, lacked the same two gliadins. All the subunits in the other thirty-one chromosome substitution lines were indistinguishable from those in ‘Chinese Spring’. It is therefore concluded that the major variation affecting gliadin and glutenins in wheat is concentrated on the chromosomes of homoeologous Groups 1 and 6 but Group 2 chromosomes are candidates for further study. An endosperm protein controlled by chromosome 4D in ‘Chinese Spring’ is shown to be a high molecular weight globulin.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00276448
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    Paper (German National Licenses)
    Fulltext
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