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  • 1
    Electronic Resource
    Electronic Resource
    Springer
    Planta 149 (1980), S. 227-233 
    ISSN: 1432-2048
    Keywords: Germination (seeds) ; Immunoprecipitation ; mRNA ; Poly(A) RNA ; Vigna
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The poly(A)-rich RNA from dry mung bean (Vigna radiata [L.] Wilczek) embryonic axes has been isolated and translated in a wheat embryo cell-free system, and the products were analyzed on sodium dodecyl sulfate-polyacrylamide gels. The fluorographyic patterns showed a heavy band at approximately MW 12,000. The messenger RNA coding for this polypeptide disappeared in the course of early germination. This messenger is translated in vivo but simultaneously degrades when the axes imbibe. The poly(A)-rich RNA from dry axes has been fractionated on sucrose-dimethyl sulfoxide gradients, and this messenger has been found to be distributed largely in the 9–14 S region. The polypeptide synthesized in vitro has been immunoprecipitated, using the antiserum raised against this protein purified from dry axes.
    Type of Medium: Electronic Resource
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  • 2
    ISSN: 1432-2048
    Keywords: Cell-free translation ; Lectin ; Long-lived mRNA ; Pisum
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Extracts prepared from dry pea (Pisum sativum, L; cv oberon) primary axes translate efficiently their endogenous messengers in an in vitro protein synthesizing system. The native long-lived messengers are biologically fully active and direct the synthesis of a whole range of polypeptides with MW ranging up to 130,000. About 0.5% of the total in vitro synthesized polypeptides are recovered in the immunoprecipitate obtained with pea lectin antiserum. Since about one-fourth of the radioactivity in the immunoprecipitate comigrates with authentic pea lectin it is concluded that about 0.1% of the long-lived messengers code for the lectin.
    Type of Medium: Electronic Resource
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  • 3
    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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  • 4
    Electronic Resource
    Electronic Resource
    Springer
    Planta 156 (1982), S. 41-44 
    ISSN: 1432-2048
    Keywords: Germination (seeds) ; Lectin ; mRNA (preformed) ; Secale (lectins) ; Seed development ; Triticum (lectins)
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Wheat (Triticum aestivum L.) and rye (Secale cereale L.) lectins are specifically synthesized during seed formation. They accumulate exponentially in the primary axes in a period coinciding with the development of this complex organ. Since the specific lectin content also increases dramatically, there is apparently an outburst of lectin synthesis during the development of the primary axes. Germinating embryos also synthesize some lectin. The fortunate availability of a highly specific procedure for the isolation of cereal lectins enabled us to follow the kinetics of their synthesis during early germination. Stored mRNAs appear to be involved in this residual lectin synthesis.
    Type of Medium: Electronic Resource
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