| | 1 | 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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