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  • 1975-1979  (2)
  • 1945-1949
  • Sulphur  (1)
  • in situ hybridization  (1)
  • 1
    Electronic Resource
    Electronic Resource
    Springer
    Planta 146 (1979), S. 463-466 
    ISSN: 1432-2048
    Keywords: Legumin ; Pisum ; Protein (seeds) ; Storage proteins ; Sulphur ; Vicilin
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract By means of crossed immunoelectrophoresis of the cotyledonary storage proteins of Pisum sativum L. it was shown that reduced accumulation of the legumin fraction, resulting from severe sulphur deficiency during growth, is accompanied by relative suppression of a quantitatively minor storage protein (Peak 3) shown previously by subunit analysis to be related to the vicilin series of holoproteins. The pattern of isotopic labelling of the storage proteins after injection of [35S]methionine into the pedicel during seed development under normal nutritional conditions indicated that Peak-3 protein, like legumin, has a relatively high content of sulphur amino-acids. Like certain of the vicilin molecules carrying the determinants responsible for Peak-4, Peak-3 protein binds selectively to concanavalin A.
    Type of Medium: Electronic Resource
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  • 2
    ISSN: 1573-4927
    Keywords: Calliphora ; calliphorin ; storage protein ; hemolymph ; fat body ; mRNA ; in vitro translation ; in situ hybridization ; structural gene
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract A major poly(A)-containing RNA fraction of the approximate size expected of a monocistronic mRNA for the storage protein calliphorin has been isolated from the larval fat bodies of Calliphora vicina during early instar 3. This 20 S RNA fraction programs the synthesis by cell-free wheat embryo extracts of polypeptides of 86,000 daltons identified by tryptic peptide fingerprinting as precursors of the authentic calliphorin subunits of 83,000 daltons. Complementary DNA synthesized by AMV reverse transcriptase using the same 20 S RNA as template hybridized in situ to a single segment of one or two bands in the salivary polytene chromosomes of C. vicina.
    Type of Medium: Electronic Resource
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