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  • 1995-1999  (2)
  • Brazil nut protein, grain legumes, leguminB4 promoter  (1)
  • Seed  (1)
  • 1
    Electronic Resource
    Electronic Resource
    Subcellular localization of the 2S globulin narbonin in seeds of Vicia narbonensis (1997)
    Springer
    Planta 203 (1997), S. 44-50 
    Details
    ISSN: 1432-2048
    Keywords: Key words: 2S Globulin ; Narbonin (immunolocalization) ; Seed ; Storage Protein ; Translation (in vitro) ; Vicia
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: 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.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s004250050163
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Seed specific expression of the 2S albumin gene from Brazil nut (Bertholletia excelsa) in transgenicVicia narbonensis (1995)
    Springer
    Molecular breeding 1 (1995), S. 295-301 
    Details
    ISSN: 1572-9788
    Keywords: Brazil nut protein, grain legumes, leguminB4 promoter ; seed storage protein ; sulphur amino acid deficiency ; transgenic plants ; Vicia narbonensis
    Source: Springer Online Journal Archives 1860-2000
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition
    Notes: Abstract In order to evaluate the possibility of enhancing the sulphur amino acids in grain legumes, we have transferred the gene for the methionine-rich 2S albumin from Brazil nut (Bertholletia excelsa) controlled by a seed-specific promoter intoVicia narbonensis. The coding region of the 2S albumin gene that has been completely synthesized was fused to the seed-specific leguminB4 promoter fromVicia faba. Transgenic lines ofV. narbonensis were generated viaAgrobacterium-mediated gene analysis of leaves, stems, roots and seeds of four R0 plants revealed that the expression of the foreign 2S albumin gene occurred in a seed-specific manner and that the foreign protein is present at levels ranging from 1% to 4.8% of total SDS-soluble seed protein. Since the current protocol for transformation ofV. narbonensis has not yet been published, a detailed description of the method is given.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02277429
    Library Location Call Number Volume/Issue/Year Availability
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    Paper (German National Licenses)
    Fulltext
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