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  • 1
    Electronic Resource
    Electronic Resource
    Control of benzylamine oxidase activity in Kluyveromyces fragilis grown on primary amines as nitrogen source (1985)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 29 (1985), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Abstract After growth on a mixture of ammonium and either methylamine or n-butylamine as nitrogen sources, benzylamine oxidase activity in yeasts from a number of different genera was found to be repressed to a lesser extent by ammonium than was methylamine oxidase. Catalase activity was better repressed by ammonium with methylamine as the nitrogen source than with n-butylamine. During growth of Kluyveromyces fragilis on equimolar mixtures of ammonium and an amine as nitrogen sources, benzylamine oxidase synthesis began during the period of exclusive growth on ammonium, and a period of simultaneous use of both nitrogen sources was observed just before the ammonium was exhausted. Addition of ammonium to cultures growing on n-butylamine as nitrogen source had no immediate repressive effect on benzylamine oxidase or catalase synthesis. However, growth on limiting ammonium in the absence of amines did give rise to low levels of amine oxidase and derepression of catalase activity. It is concluded that benzylamine oxidase in yeasts is induced strongly by amines as well as being less strongly repressed by ammonium than methylamine oxidase.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-6968.1985.tb00842.x
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  • 2
    Electronic Resource
    Electronic Resource
    A new type of methylamine oxidase: The sole oxidase produced during growth of Sporobolomyces albo-rubescens on primary alkylamines (1986)
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 2 (1986), S. 87-92 
    Details
    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
    URL: http://dx.doi.org/10.1002/yea.320020203
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    Paper (German National Licenses)
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