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  • Nitrate reductase  (2)
  • l-amino-acid oxidase (molecular properties)  (2)
  • Enzyme purification
  • Springer  (4)
  • 1
    Electronic Resource
    Electronic Resource
    Purification and characterization of anl-amino-acid oxidase fromChlamydomonas reinhardtii (1992)
    Springer
    Planta 188 (1992), S. 13-18 
    Details
    ISSN: 1432-2048
    Keywords: l-amino-acid oxidase (molecular properties) ; Chlamydomonas (l-amino-acid oxidase) ; Flavoprotein
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Anl-amino-acid oxidase (EC 1.4.3.1) that catalyzes the oxidative deamination of twelvel-amino acids has been purified 21-fold and with 14% yield to electrophoretic homogeneity fromChlamydomonas reinhardtii cells by ammonium-sulfate fractionation, gel filtration through Sephacryl and Superose, anion-exchange chromatography and preparative electrophoresis in polyacrylamide gels. The native enzyme is a protein of 470 kDa and consists of eight identical or similarsized subunits of 60 kDa each. Optimum pH and temperature were 8.2 and 55° C, respectively, with a Q10 (45–55° C) of 1.7 and an activation energy of 45 kJ · mol−1. Its absorption spectrum showed, in the visible region, maxima at 360 and 444 nm, characteristic of a flavoprotein with a calculated flavin content of 7.7 mol FAD per mol of native enzyme. ApparentK m values of the twelvel-amino acids which can act as substrates ofl-amino-acid oxidase ranged between 31 μM for phenylalanine and 176 μM for methionine. The effect of several specific group reagents, chelating agents and bivalent cations on enzyme activity has also been studied.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01160707
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  • 2
    Electronic Resource
    Electronic Resource
    Assimilatory nitrate reductase from Acinetobacter calcoaceticus (1977)
    Springer
    Archives of microbiology 112 (1977), S. 127-132 
    Details
    ISSN: 1432-072X
    Keywords: Acinetobacter calcoaceticus ; Nitrate reductase ; Interconversion ; Cyanate ; Enzyme synthesis
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract A soluble nitrate reductase from the bacterium Acinetobacter calcoaceticus grown on nitrate has been characterized. The reduction of nitrate to nitrite is mediated by an enzyme of 96000 molecular weight that can use as electron donors either viologen dyes chemically reduced with dithionite or enzymatically reduced with NAD(P)H, through specific diaphorases which utilize viologens as electron acceptors. Nitrate reductase activity is molybdenum-dependent as shown by tungstate antagonistic experiments and is sensitive to -SH reagents and metal chelators such as KCN. The enzyme synthesis is repressed by ammonia. Moreover, nitrate reductase activity undergoes a quick inactivation either by dithionite and temperature or by dithionite in the presence of small amounts of nitrate. Cyanate prevents this inactivating process and can restore the activity once the inactivation had occurred, thus suggesting that an interconversion mechanism may participate in the regulation of Acinetobacter nitrate reductase.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00429324
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  • 3
    Electronic Resource
    Electronic Resource
    Purification and characterization of an l-amino-acid oxidase from Chlamydomonas reinhardtii (1992)
    Springer
    Planta 188 (1992), S. 13-18 
    Details
    ISSN: 1432-2048
    Keywords: l-amino-acid oxidase (molecular properties) ; Chlamydomonas (l-amino-acid oxidase) ; Flavoprotein
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract An l-amino-acid oxidase (EC 1.4.3.1) that catalyzes the oxidative deamination of twelve l-amino acids has been purified 21-fold and with 14% yield to electrophoretic homogeneity from Chlamydomonas reinhardtii cells by ammonium-sulfate fractionation, gel filtration through Sephacryl and Superose, anion-exchange chromatography and preparative electrophoresis in polyacrylamide gels. The native enzyme is a protein of 470 kDa and consists of eight identical or similarsized subunits of 60 kDa each. Optimum pH and temperature were 8.2 and 55° C, respectively, with a Q10 (45–55° C) of 1.7 and an activation energy of 45 kJ · mol−1. Its absorption spectrum showed, in the visible region, maxima at 360 and 444 nm, characteristic of a flavoprotein with a calculated flavin content of 7.7 mol FAD per mol of native enzyme. Apparent K m values of the twelve l-amino acids which can act as substrates of l-amino-acid oxidase ranged between 31 μM for phenylalanine and 176 μM for methionine. The effect of several specific group reagents, chelating agents and bivalent cations on enzyme activity has also been studied.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00198934
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  • 4
    Electronic Resource
    Electronic Resource
    Occurrence of xanthine dehydrogenase in Chlamydomonas reinhardii: A common cofactor shared by xanthine dehydrogenase and nitrate reductase (1981)
    Springer
    Planta 153 (1981), S. 254-257 
    Details
    ISSN: 1432-2048
    Keywords: Chlamydomonas (mutants) ; Nitrate reductase ; Xanthine dehydrogenase
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Wild-type Chlamydomonas reinhardii cells have xanthine dehydrogenase activity when grown with nitrate, nitrite, urea, or amino acid media. Mutant strains 102, 104, and 307 of Chlamydomonas, lacking both xanthine dehydrogenase and nitrate reductase activities, were incapable of restoring the NADPH-nitrate reductase activity of the mutant nit-1 of Neurospora crassa, whereas wild type cells and mutants 203 and 305 had xanthine dehydrogenase and were able to reconstitute the nitrate reductase activity of nit-1 of Neurospora. Therefore, it is concluded that in Chlamydomonas a common cofactor is shared by xanthine dehydrogenase and nitrate reductase. Xanthine dehydrogenase is repressed by ammonia and seems to be inessential for growth of Chlamydomonas.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00383895
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