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  • Vicia faba  (2)
  • 25.70  (1)
  • Gene evolution  (1)
  • 1
    Digitale Medien
    Digitale Medien
    Legumin-like and vicilin-like seed storage proteins: Evidence for a common single-domain ancestral gene (1995)
    Springer
    Journal of molecular evolution 41 (1995), S. 1057-1069 
    Details
    ISSN: 1432-1432
    Schlagwort(e): Gene evolution ; Seed protein genes ; Legumin ; Vicilin ; Gene family ; Sequence homology ; Intron/exon structure
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Biologie
    Notizen: Abstract Legumin-like 11S and vicilin-like 7S globulins are the main storage proteins of most angiosperms and gymnosperms. The subunits of the hexameric legumin are synthesized as a precursor comprising a N-terminal acidic α- and a C-terminal basic β-chain. The trimeric vicilin molecule consists of subunits composed of two symmetrical N- and C-terminal structural domains. In a multiple alignment we have compared the N-terminal and C-terminal domains of 11 legumns and seven vicilins of several dicot, monocot, and gymnosperm species. The comparisons using all six possible pairwise combinations reveal that the N-terminal and C-terminal domains of both protein families are similar to each other. These results together with data on the distribution of variable and conserved regions, on the positions of susceptible sites for proteolytic attack, as well as on the published 7S protein tertiary structure suggest that both protein families share a common single-domain ancestor molecule and lead to the hypothesis that a triplication event has occurred during the evolution of a putative legumin/vicilin ancestor gene. Moreover, the comparison of the intron/exon pattern reveals that at least three out of five intron positions are precisely conserved between the genes of both protein families, further supporting the idea of a common evolutionary origin of recent legumin and vicilin encoding genes.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1007/BF00173187
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  • 2
    Digitale Medien
    Digitale Medien
    Polymorphism of legumin subunits from field bean (Vicia faba L. var. minor) and its relation to the corresponding multigene family (1993)
    Springer
    Theoretical and applied genetics 86 (1993), S. 867-874 
    Details
    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
    URL: http://dx.doi.org/10.1007/BF00212614
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  • 3
    Digitale Medien
    Digitale Medien
    Subthreshold kaon production in Au on Au collisions at 1 GeV/u (1991)
    Springer
    The European physical journal 341 (1991), S. 123-124 
    Details
    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
    URL: http://dx.doi.org/10.1007/BF01281285
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  • 4
    Digitale Medien
    Digitale Medien
    Stable expression of vicilin fromVicia faba with eight additional single methionine residues but failure of accumulation of legumin with an attached peptide segment in tobacco seeds (1995)
    Springer
    Molecular breeding 1 (1995), S. 245-258 
    Details
    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
    URL: http://dx.doi.org/10.1007/BF02277425
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