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  • Vicia faba  (2)
  • 25.70  (1)
  • Key words: 2S Globulin  (1)
  • 1
    ISSN: 1432-2048
    Schlagwort(e): Key words: 2S Globulin ; Narbonin (immunolocalization) ; Seed ; Storage Protein ; Translation (in vitro) ; Vicia
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Biologie
    Notizen: Abstract. Narbonin is a 2S protein from the globulin fraction of narbon bean (Vicia narbonensis L.) cotyledons. Its amino acid composition and the pattern of its regulated accumulation in developing seeds led to the suggestion that narbonin could be a storage protein. Therefore, it was expected to be present in protein bodies of the storage tissue cells. Comparison of the cDNA-derived amino acid sequence with a directly determined partial N-terminal sequence revealed that the primary translation product of narbonin mRNA lacks a transient N-terminal signal peptide (V.H. Nong et al., 1995, Plant Mol Biol 28: 61–72). Narbonin polypeptides that had been synthesized in a cell-free translation system supplemented with dog pancreas microsomes were not protected against degradation by posttranslationally added proteases (protease protection assay). In accordance with the lack of a signal peptide this indicates that the polypeptide was not cotranslationally sequestered into the microsomes. The protein-body fraction that had been isolated from mature narbon bean cotyledons by a non-aqueous gradient centrifugation procedure was free of narbonin; this was found in the soluble cell fraction. In electron micrographs, narbonin could be localized in the cytoplasm using the immuno gold-labelling technique. Previously, it had already been shown that narbonin is too slowly degraded during narbon bean germination to act as a storage protein. From all these results it has to be concluded that narbonin is a cytoplasmic protein which does not belong to the storage proteins in the restricted sense. Other possible functions are discussed.
    Materialart: Digitale Medien
    Bibliothek Standort Signatur Band/Heft/Jahr Verfügbarkeit
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  • 2
    ISSN: 1432-2242
    Schlagwort(e): cDNA ; Legumin subunits ; Polymorphism ; Gene assignment ; Vicia faba
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Biologie
    Notizen: 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.
    Materialart: Digitale Medien
    Bibliothek Standort Signatur Band/Heft/Jahr Verfügbarkeit
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  • 3
    ISSN: 1434-601X
    Schlagwort(e): 25.70 ; 21.65
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Physik
    Notizen: Abstract Subthreshold kaon production in197 Au+197 Au collisions at 1.0 GeV/u has been investigated with the Kaon Spectrometer at SIS. At Θ lab =44±4∘ we found aK +/p ratio of〉3 · 10−4 for the momentum range 650 MeV/c to 1150 MeV/c.
    Materialart: Digitale Medien
    Bibliothek Standort Signatur Band/Heft/Jahr Verfügbarkeit
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  • 4
    ISSN: 1572-9788
    Schlagwort(e): legumin ; methionine ; modification ; nutritional value ; Vicia faba ; vicilin
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Land- und Forstwirtschaft, Gartenbau, Fischereiwirtschaft, Hauswirtschaft
    Notizen: Abstract Two different attempts have been undertaken to improve the amino acid composition of storage proteins from field bean (Vicia faba) by genetic engineering. First, legumin was modified to generate a new peptide sequence at the C-terminus containing 4 methionine residues. Second, vicilin was modified by generating 8 single methionine residues distributed over the peptide sequence. The genes were expressed in different systems includingin vitro transcription and translation and stable transformation into tobacco. The modified legumin was found to be unstable when expressed in tobacco seeds. Although specific mRNA was detected on RNA gel blots, no protein could be found by using protein gel blotting and ELISA. Furthermore, a protease preparation able to process the original legumin precursorin vitro degraded the modified legumin precursor. Contrary, the modified vicilin was accumulated in seeds of tobacco transformed with the gene under the control of the seed specific USP promoter. Both the original and the modified vicilin could be detected on protein gel blots at the expected position. Two-dimensional electrophoresis was employed to analyse the expression of original vicilin. Three vicilin-specific products of almost equal size were observed, indicating a slight modification leading to a change of pI. Quantitative determination using competitive ELISA showed that there is no significant difference in accumulation between original and modified vicilin. In both cases, three plants were found with vicilin amounts in the range of 1–3% of total globulin.
    Materialart: Digitale Medien
    Bibliothek Standort Signatur Band/Heft/Jahr Verfügbarkeit
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