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  • Ammonium assimilation  (1)
  • NH 4 + assimilation  (1)
  • Analytical Chemistry and Spectroscopy
  • Nuclear Reactions
  • 1980-1984  (1)
  • 1983  (1)
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  • 1980-1984  (1)
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  • 1
    Electronic Resource
    Electronic Resource
    Springer
    Planta 159 (1983), S. 483-486 
    ISSN: 1432-2048
    Keywords: Ammonium assimilation ; Glutamate dehydrogenase ; Hordeum ; NH 4 + assimilation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Enzyme assays of the roots of barley (Hordeum vulgare L.) fed NH 4 + show high glutamate-dehydrogenase (GDH; EC 1.4.1.3) activity compared with glutamine-synthetase (GS; EC 6.3.1.2) activity, indicating that GDH may be involved in ammonium assimilation in the root. When 15NH 4 + is fed to barley roots, a high accumulation of 15N takes place in free amino compounds, particularly glutamine and glutamate. When the GS inhibitor, methionine sulfoximine (MSO), is added to the 15NH 4 + feeding medium the free amino compounds remain unlabelled while 15NH 4 + accumulates rapidly in the roots. Root enzyme assays demonstrate that GS is completely inhibited by MSO treatment, while the activity of GDH remains unaffected. The feeding of 15N-amido glutamine to the roots in the presence of MSO and the subsequent 15N enrichment of the free amino compounds of the root show that MSO does not interfere substantially with nitrogen assimilation after the formation of glutamine. These results indicate that in the barley root, ammonium absorbed from the soil is assimilated entirely via the GS-glutamate synthase (GOGAT) pathway, and that GDH plays little, if any, part in this process.
    Type of Medium: Electronic Resource
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