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  • 75.60  (3)
  • Chlamydomonas (l-amino-acid oxidase)  (2)
  • Springer  (5)
  • 1
    Electronic Resource
    Electronic Resource
    Comparison between disaccommodation and ferromagnetic resonance measurements in polycrystalline nickel ferrites (1995)
    Springer
    Applied physics 60 (1995), S. 303-307 
    Details
    ISSN: 1432-0630
    Keywords: 76.50 ; 75.60
    Source: Springer Online Journal Archives 1860-2000
    Topics: Mechanical Engineering, Materials Science, Production Engineering, Mining and Metallurgy, Traffic Engineering, Precision Mechanics , Physics
    Notes: Abstract FerroMagnetic Resonance (FMR) measurements of polycrystalline nickel ferrites at 11 GHz from 77 to 400 K have been carried out. The different contributions to the FMR linewidth have been studied by a computational technique based on the parameters previously obtained for single-crystal nickel ferrite. A new qualitative comparison between the FMR and disac-commodation measurements by means of the induced anisotropy formalism is presented.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01538408
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  • 2
    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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  • 3
    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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  • 4
    Electronic Resource
    Electronic Resource
    Magnetic disaccommodation in normal spinel structures (1991)
    Springer
    Applied physics 52 (1991), S. 242-246 
    Details
    ISSN: 1432-0630
    Keywords: 75.60 ; 76
    Source: Springer Online Journal Archives 1860-2000
    Topics: Mechanical Engineering, Materials Science, Production Engineering, Mining and Metallurgy, Traffic Engineering, Precision Mechanics , Physics
    Notes: Abstract Magnetic disaccommodation is investigated for ferrous ferrites with normal spinel structure. This study shows the presence of a new relaxation process in the temperature region IV (≃285 K) that has not been detected in inverse spinels. A numerical analysis of the isochronal spectra reveals that it is composed of two simple Debye processes with activation energies close to 0.75 eV and 0.80 eV, and preexponential factors 3×10−13 s. This relaxation is attributed to the formation of an induced anisotropy due to jumps of B-Fe ions into vacancies (as process III), but in presence of a divalent cation occupying an A-site.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00324585
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  • 5
    Electronic Resource
    Electronic Resource
    Micromagnetic model of the Richter-type relaxation in vacancy-doped Fe3O4 (1986)
    Springer
    Applied physics 39 (1986), S. 287-289 
    Details
    ISSN: 1432-0630
    Keywords: 75.60 ; 76
    Source: Springer Online Journal Archives 1860-2000
    Topics: Mechanical Engineering, Materials Science, Production Engineering, Mining and Metallurgy, Traffic Engineering, Precision Mechanics , Physics
    Notes: Abstract Isothermal disaccommodation curves in vacancy-doped magnetite at room temperature show a typical Richter-type behaviour. Magnetic susceptibility decreases asymptotically according to a relaxation time of about 102 s, which is analyzed in terms of a progressive stabilization of the domains walls. The relaxation strength, vacancies and the restoring pressure on the Bloch walls are closely related.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00617274
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