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  • Legumin subunits  (1)
  • Vicia (protein bodies)  (1)
  • 1
    Electronic Resource
    Electronic Resource
    Springer
    Planta 157 (1983), S. 401-410 
    ISSN: 1432-2048
    Keywords: Protein body ; Seed development ; Storage protein ; Vacuole ; Vicia (protein bodies)
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Storage proteins of the field bean (Vicia faba L., var. minor, cv. “Fribo”) are synthesized and accumulated in the cotyledons during stage 2 of seed development. Deposition of protein reserves takes place in the protein bodies. The generation of protein bodies was investigated electronmicroscopically using ultra-thin sections as well as the freeze-fracturing technique. During the initial period of storage protein formation, globulins are deposited in large vacuoles which later are transformed to give increasing numbers of small vacuoles with decreasing size. The vacuoles disappear early during the stage of storage protein formation and generate the first protein bodies. During the subsequent period of maximum storage protein formation, which takes place at the rough endoplasmic reticulum (rER), swollen ER strands appear which seem to be entirely filled with protein, and these generate ER-produced protein vacuoles (ERPVAC). The vesicles are transformed in a manner comparable to the vacuoles in the initial period of developmental stage 2 and thus generate the major quantity of protein bodies. Both processes seem to represent only two variants of an uniform mechanism of protein body generation.
    Type of Medium: Electronic Resource
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  • 2
    ISSN: 1432-2242
    Keywords: cDNA ; Legumin subunits ; Polymorphism ; Gene assignment ; Vicia faba
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Legumin, which amounts to approximately 55% of the seed protein in field beans (Vicia faba L. var. minor), is a representative of the 12S storage globulin family. The 12S storage globulins are hexameric holoprotein molecules composed of different types of polymorphic subunits encoded by a multigene family. ‘Type-A’ legumin subunits contain methionine whereas ‘type-B’ are methionine-free subunits. Sequencing of two different type A-specific cDNAs, as well as an FPLC/HPLC-based improvement of subunit fractionation and peptide mapping with subsequent partial amino-acid sequencing, permit the assignment of some of the polymorphic legumin subunits to members of the multigene family. Two different type A subunits (A1 and A2) correspond to the two different cDNA clones pVfLa129 (A2) and 165 (A1), but microheterogeneity in the amino-acid sequences indicates that polymorphic variants of both representatives of this type may exist. Two groups of published type B-specific gene sequences (LeB7, and LeB2, LeB4, LeB6, respectively) are represented by two polymorphic subunit fractions (B3I, B3II, and B4I, B4II). A seventh clone, LeB3, encodes one of the large legumin subunits that is only a minor component of the legumin seed protein complex.
    Type of Medium: Electronic Resource
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