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'Ammonium Assimilation' in keywords Facet   section ZfN Section C  [X]
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1989 (1)
1982 (1)
1981 (1)
1Author    Aloysius Wild, Christine ZieglerRequires cookie*
 Title    The Effect of Bialaphos on Ammonium-Assimilation and Photosynthesis I. Effect on the Enzymes of Ammonium-Assimilation  
 Abstract    In this investigation, the effect of bialaphos (phosphinothricyl-alanyl-alanine) on the enzymes involved in NH4+-assimilation — glutamine synthetase, glutamine-2-oxoglutarate aminotrans­ ferase, glutamate dehydrogenase — is examined and compared to the effect of phosphinothricin (glufosinate) on the same enzymes. Bialaphos was given to whole plants (in vivo) and to leaf homogenate (in vitro). The investigation showed that bialaphos has an inhibiting effect on glutamine synthetase in vivo, but not in vitro. In contrast to this, phosphinothricin inhibits glutamine synthetase in vitro as well as in vivo. It was found that bialaphos, similar to phosphinothricin, does not inhibit glutamine-2-oxoglutarate aminotransferase and glutamate dehydrogenase in vivo or in vitro. Only at bialaphos concentrations exceeding 10 mM, there is an inhibition of glutamate dehydrogenase in vitro. Using radioactive ['Hjbialaphos (phosphinothricyl-'H-alanyl-alanine) it could be demonstrated that in the plant, bialaphos is split into phosphinothricin and alanine. The phosphinothricin released is probably the active herbicide component. Consequently, the herbicidal effects of phosphinothricin and bialaphos are the same. In troduction 
  Reference    Z. Naturforsch. 44c, 97 (1989); received September 23 1988 
  Published    1989 
  Keywords    Ammonium-Assimilation, Bialaphos, Glutamine Synthetase Herbicide Phosphinothricin 
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 TEI-XML for    default:Reihe_C/44/ZNC-1989-44c-0097.pdf 
 Identifier    ZNC-1989-44c-0097 
 Volume    44 
2Author    Peter Müller, DietrichW. ErnerRequires cookie*
 Title    Rhizobium japonicum  
 Abstract    Alanine dehydrogenase (E.C. 1.4.1.1.) from nitrogenase repressed free living cells o f Rhizobium japonicum 61-A-101 was purified 370 fold to a specific activity o f 30.4 (imol pyruvate • min-1 • mg protein-1. The same enzyme from effective bacteroids from nodules o f Glycine max var. Mandarin, infected with the same strain was purified 150 fold to a specific activity o f 35 units. The enzyme from both preparations was identical in the molecular weight o f about 168 kD with four identical subunits of 42 kD. The alanine dehydrogenase is, therefore, different from the same enzyme from Bacillus subtilis (molecular weight 228 kD) and from Anabaena cylindrica (molec­ ular weight 270 kD). The K m data for the enzyme from Rhizobium japonicum are: 4.7 mmol/1 for NH+, 0.68 mmol/1 for pyruvate and 44 nmol/1 for NADH. Specific activity o f the enzyme in total cell extracts from eight other strains of Rhizobium japonicum (3 effective strains, 5 ineffective strains) was only 20 to 30% o f the activity with strain 61-A -101. N o correlation between alanine dehydrogenase activity and nitrogenase activity in these other eight strains was observed. The function of alanine dehydrogenase in Rhizobium japonicum in ammonium assimilation and cell wall differentiation is discussed. 
  Reference    Z. Naturforsch. 37c, 927 (1982); received May 19 1982 
  Published    1982 
  Keywords    Rhizobium, Bacteroid Differentiation, Alanine Dehydrogenase, Glutamate Dehydrogenase, Ammonium Assimilation 
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 TEI-XML for    default:Reihe_C/37/ZNC-1982-37c-0927.pdf 
 Identifier    ZNC-1982-37c-0927 
 Volume    37 
3Author    Kassem Alef, Hans-Joachim Burkardt, Hans-Joachim Horstmann, WalterG. ZumftRequires cookie*
 Title    Molecular Characterization of Glutamine Synthetase from the Nitrogen-Fixing Phototrophic Bacterium Rhodopseudomonas palustris1  
 Abstract    The phototrophic bacterium Rhodopseudomonas palustris assimilated ammonium via glutamine synthetase and glutamate synthase. Diazotrophic and ammonium-grown cells had high levels of both enzymes, whereas enzymes o f alternative assimilatory pathways were absent or had only low activities. Glutamine synthetase was purified to electrophoretic homogeneity within three steps by dye-ligand and ion exchange chromatography. Electron microscopy revealed a dodecameric molecular entity which was in accordance with parameters derived from electrophoretic techniques. The molecular weight of the enzyme monomer was 55800; that o f the dodecamer 670000. The amino acid composition o f R. palustris glutamine synthetase was determined and compared by a statistical method with other known enzyme compositions from prokaryotic and eukaryotic origins. 
  Reference    Z. Naturforsch. 36c, 246—254 (1981); received December 231980 
  Published    1981 
  Keywords    Rhodopseudomonas palustris, Glutamine Synthetase, Dye-Ligand Chromatography, Nitrogen Fixation, Ammonium Assimilation 
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 TEI-XML for    default:Reihe_C/36/ZNC-1981-36c-0246.pdf 
 Identifier    ZNC-1981-36c-0246 
 Volume    36