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  • 1
    ISSN: 1432-2048
    Keywords: Dormancy ; Phycomyces ; Spores ; Trehalose
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Evidence is obtained for the existence of two different localizations of trehalase (α,α-trehalose glucohydrolase, EC 3.2.1.28) in Phycomyces spores: one inside the cell, and one in the periplasmic region. The latter enzyme is sensitive to 0.1 mol l-1 HCl treatment and its activity can be regulated by external pH changes. The periplasmic form of the enzyme is involved in the metabolism of added labelled trehalose. This sugar is hydrolyzed externally to glucose which is found mainly in the incubation medium and which is partly absorbed by the spores. During incubation trehalose leaks out from both dormant and activated spores and is subsequently hydrolyzed to glucose. The intracellular trehalase is probably involved in the breakdown of endogenous trehalose in spores. After heat activation the hydrolysis of endogenous trehalose is stimulated even without an important increase in activity of intracellular trehalase. Additional treatments which break dormancy of spores without a significant activation of trehalase are the following: heating of HCl-treated spores and treatment of spores with reducing substances (e.g. Na2S2O4 and NaHSO3).
    Type of Medium: Electronic Resource
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  • 2
    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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  • 3
    Electronic Resource
    Electronic Resource
    Springer
    Archives of microbiology 113 (1977), S. 95-97 
    ISSN: 1432-072X
    Keywords: Phycomyces ; Spore activation ; Dormancy ; Gamma rays
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Dormant sporangiospores of Phycomyces blakesleeanus were activated by Cs-137 gamma rays. After a dose of about 300 krad, between 80 and 90% of the spores germinated normally. However, further development of the mycelium was inhibited. Even with dry spores a partial activation was obtained. Activation by gamma rays was not accompanied by an increase in trehalase activity.
    Type of Medium: Electronic Resource
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  • 4
    Electronic Resource
    Electronic Resource
    Springer
    Planta 154 (1982), S. 568-572 
    ISSN: 1432-2048
    Keywords: Heteromeric lectin ; Hordeum ; Lectin ; Secale ; Triticale ; Triticum (lectins)
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Lectins from Triticum monococcum, Secale cereale (rye), and Hordeum vulgare (barley) can exchange their subunits in vitro and thereby form (intergeneric) heteromeric lectins. An analysis of the isolectin pattern of a Triticale variety revealed that intergeneric heterodimers of wheat and rye lectin subunits are normal constituents of the embryo cells. It appears, therefore, that these different cereal lectins are structurally so closely related that their subunits can not distinguish between identical and nonidentical partners when they associate into dimers.
    Type of Medium: Electronic Resource
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