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  • 1
    Electronic Resource
    Electronic Resource
    Springer
    Journal of molecular evolution 7 (1976), S. 159-165 
    ISSN: 1432-1432
    Keywords: Nitrogenases ; ATP-ases ; Amino Acid Compositions ; S△Q ; Evolutionary Relationships
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary Comparisons of the amino acid compositions of the nitrogenase proteins from different organisms and their correlation with cross-reactivities and taxonomical data suggest an evolution within bacterial genomes rather than within plasmids. Comparisons of the amino acid compositions of nitrogenases and other ATP-ases show similarities which might be due to the evolution of these ATP-ases from a common ancestral protein.
    Type of Medium: Electronic Resource
    Library Location Call Number Volume/Issue/Year Availability
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  • 2
    Electronic Resource
    Electronic Resource
    Springer
    Archives of microbiology 128 (1981), S. 412-415 
    ISSN: 1432-072X
    Keywords: Nitrogenase ; Glutamine synthetase ; Repression ; Amino acid pools ; Adenine nucleotide pools ; Azolobacter vinelandii
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract When continuous cultures of Azotobacter vinelandii were supplied with ammonium or nitrate in amounts, which just repressed nitrogenase synthesis completely, both the intracellular glutamine level and the degree of adenylylation of the glutamine synthetase (GS) increased only slightly (from 0.45–0.50 mM and from 2 to 3 respectively), while the total GS level remained unaffected. Higher amounts of ammonium additionally inhibited the nitrogenase activity, caused a strong rise in the intracellular glutamine concentration and adenylylation of the GS, but caused no change in the ATP/ADP ratio. These results are considered as evidence that in A. vinelandii the regulation of nitrogenase synthesis is not linked to the adenylylation state of the GS and to the intracellular glutamine level, and that the inhibition of the nitrogenase activity as a consequence of a high extracellular ammonium level is not mediated via a change in the energy charge.
    Type of Medium: Electronic Resource
    Library Location Call Number Volume/Issue/Year Availability
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