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  • 1
    Electronic Resource
    Electronic Resource
    Chichester [u.a.] : Wiley-Blackwell
    Developmental Genetics 9 (1988), S. 215-226 
    ISSN: 0192-253X
    Keywords: cAMP ; cGMP ; chemotaxis ; mutant ; desensitization ; receptor ; Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: The functional interaction of surface cAMP receptors with effector enzymes via G-proteins was investigated in Dictyostelium discoideum. Several experimental conditions were used to investigate signal transduction, such as reduced temperatures, use of down-regulated cells and of mutants. The results are presented as a model describing the complex interaction between multiple forms of the surface cAMP receptor and different G-proteins that are responsible for the generation of the second messengers, cAMP, cGMP, InsP3 and Ca2+.
    Additional Material: 7 Ill.
    Type of Medium: Electronic Resource
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  • 2
    ISSN: 0192-253X
    Keywords: Drosophila ; temperature effects ; heat-shock ; cell-lethal mutation ; Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Pulses of various durations at temperatures between 29 and 38°C were applied to developing larvae of Drosophila melanogaster carrying the temperature-sensitive cell-lethal mutation 1 (1)ts726. The results show that it is not possible to reduce the time required for the induction of abnormalities in the mutant by treating larvae with heat pulses at temperatures higher than 29°C. Instead, treatment with high temperature leads to fewer abnormalities than 29°C treatments. Furthermore with high temperature treatments, the mutation has less effect on viability than is seen at 29°C. It is suggested that 1 (1)ts726 leads to abnormalities and death by a temperature-induced imbalance between different physiological or development events, rather than by interfering with the ability of the cell or the organism to withstand high temperature in general.
    Additional Material: 5 Ill.
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  • 3
    Electronic Resource
    Electronic Resource
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 2 (1986), S. 1-34 
    ISSN: 0749-503X
    Keywords: Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Additional Material: 11 Ill.
    Type of Medium: Electronic Resource
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  • 4
    ISSN: 0749-503X
    Keywords: Aminotransferase ; transaminase ; 4-aminobutyrate ; Candida ; putrescine ; spermidine ; cytisol ; Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: 4-Aminobutyrate aminotransferase (EC 2.6.1.19) was elevated in activity by 20- to 40-fold in cells of the yeast Candida boidinii grown on spermidine, putrescine, 4-acetamidobutyrate and 4-aminobutyrate compared with activities detected in cells grown on ammonium, methylamine or 6-aminohexanoate, confirming previous suggesions that it plays a key role in polyamine breakdown. Other enzymes of the proposed route of polymine breakdown were found to be non-coordinately induced or derepressed during growth on spermidine or its putative breakdown intermediates. The enzyme was not sedimented from spheroplast lysates at 100 000 × g, and it is concluded that it is conclded that it is probably cytosoilc in its subcellular location (although the data do not exclude the possiblity of its being vacuolar).
    Additional Material: 2 Tab.
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  • 5
    ISSN: 0749-503X
    Keywords: Amine oxidase ; yeast ; methylamine ; n-butylamine ; Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Under conditions known to separate methylamine oxidase from benzylamine oxidase in other yeast strains, only a single oxidase could be detected in Sporobolomyces albo-rubescens. This occurred irrespective of whether methylamine or n-butylamine was the nitrogen source for growth. The oxidase did not attack benzylamine. It was concluded that this organism can only produce a methylamine oxidase. The enzyme was purified to 90% homogeneity and found to have properties significantly a methylamine oxidases previously characterised. It lost only 40% of its activity in 30 min at 45°C, whereas methylamine oxidase previously described had half-lives of from 2 to 9 min at 45°C. It showed also a lower activity with short chain 1-aminoalkanes and a higher activity with longer chain 1-aminoalkanes than other methylamine oxidases, and had a significantly smaller subunit molecular weight (57 000 compared with 80 000).
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
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