| | 1 | Author
| Aloysius Wild, Christine Ziegler | Requires 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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| default:Reihe_C/44/ZNC-1989-44c-0097.pdf | | | | Identifier
| ZNC-1989-44c-0097 | | | | Volume
| 44 | |
| 2 | Author
| Peter Müller, DietrichW. Erner | Requires 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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| default:Reihe_C/37/ZNC-1982-37c-0927.pdf | | | | Identifier
| ZNC-1982-37c-0927 | | | | Volume
| 37 | |
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