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  • 1
    Electronic Resource
    Electronic Resource
    Springer
    Planta 147 (1980), S. 307-311 
    ISSN: 1432-2048
    Keywords: Embryo ; Protein synthesis ; Scutellum ; Secale ; Translation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Some botanical aspects of cell-free protein synthesizing systems from cereal embryos have been investigated. The composition of the starting material determines both the stability and translation fidelity of the cell-free extracts. The active components of the extracts originate exclusively from the primary axes. Contamination with scutellum fragments does not affect the initial activity but results in a reduced stability. The presence of endosperm particles in the starting material leads to a strong decrease of the overall activity of the extracts and a loss of the capacity to synthesize large polypeptides.
    Type of Medium: Electronic Resource
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  • 2
    ISSN: 1432-2048
    Keywords: Cell-free translation ; Preformed mRNA ; Rye embryos ; Sedimentation behavior
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Two classes of messenger containing particles can be distinguished in cell-free extracts from dry rye (Secale cereale, L.; var. Celestijner) embryos. A part of the endogenous template activity is associated with large structures, even during in vitro translation. Treatment with detergents results in a partial solubilization of the messenger particles from the large, presumably membranous structures. The sedimentation behavior of the “soluble” mRNP particles (about 75% of the total endogenous template activity) is strongly influenced by the composition of the homogenization medium. At high Mg2+ or Ca2+ concentrations, and at low pH, the soluble mRNP particles form aggregates sedimenting at low centrifugal forces. This peculiar behavior is of partical interest with respect to the preparation of cell-free extracts with low endogenous template activity.
    Type of Medium: Electronic Resource
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  • 3
    ISSN: 1432-2048
    Keywords: Embryo (mRNA) ; Messenger ribonucleoprotein ; mRNA ; Ribonucleoprotein (messenger) ; Secale ; Seed development
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Untranslated messenger ribonucleoproteins (mRNPs informosomes) are present in developing rye (Secale cereale, L. cv. Celestijner) embryos throughout the last 5 weeks of seed formation. Ribosomal as well as non-ribosomal ribonucleoproteins are formed continuously both in primary axes and scutella until any synthesis of macromolecules stops upon dessication. The content of preformed messengers in the primary axes of precociously harvested rye grains increases as a function of embryo development. This increase of the “template load” of the primary axes results from a continuous accumulation of qualitatively identical mRNPs. Germination experiments demonstrated that at least most of the preformed messengers are not required for the germination process. Their function is discussed in terms of selective adaptation to unfavorable conditions.
    Type of Medium: Electronic Resource
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  • 4
    Electronic Resource
    Electronic Resource
    Springer
    Planta 144 (1979), S. 491-496 
    ISSN: 1432-2048
    Keywords: Embryo (mRNA) ; Germination (embryo) ; Messenger ribonucleoprotein ; mRNA ; Ribonucleoprotein (messenger) ; Translation ; Triticum
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract In 6 h germinated wheat (Triticum aestivum L. cv. Cama) embryos, more than half of the messenger RNAs are actively involved in translation. Neither preformed nor newly synthesized poly A+-RNA is translated preferentially. Germination in the presence of cordycepin showed that the half-life of the templates is about 2 h and that the newly synthesized messengers are essential to support protein synthesis in the embryo from the first hours of germination. Most of the messenger RNAs in 6 h germinated embryos are newly synthesized. The polypeptides coded for by either the endogenous messenger ribonucleoproteins or purified poly A+-RNA from both dry and germinated embryos are qualitatively identical; minor quantitative differences can however be observed.
    Type of Medium: Electronic Resource
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