Glutamate Dehydrogenase from Apodachlya (Oomycetes)
نویسندگان
چکیده
منابع مشابه
Ox liver glutamate dehydrogenase
1. The effect of pyridoxal 5'-phosphate on the activity of ox liver glutamate dehydrogenase towards different amino acid substrates was investigated. 2. Both alanine and glutamate activities decreased steadily in the presence of pyridoxal 5'phosphate. 3. The alanine/glutamate activity ratio increased as a function of inactivation by pyridoxal 5'-phosphate, indicating that glutamate activity is ...
متن کاملRegulation of Bovine Glutamate Dehydrogenase
The activity of bovine liver glutamate dehydrogenase is affected in several ways depending on substrate concentrations and pH. At pH 6.5 and below, both oxidative deamination and reductive amination reactions are inhibited by ADP. At pH 7.0 and above both activatory and inhibitory effects can be observed depending on substrate concentrations. The effects are explicable in terms of a model with ...
متن کاملGlutamate dehydrogenase from the thermoacidophilic archaebacterium Sulfolobus solfataricus.
An NAD(P)-dependent glutamate dehydrogenase was purified to homogeneity from the thermoacidophilic archaebacterium Sulfolobus solfataricus. The enzyme is a hexamer (subunit mass 45 kDa) which dissociates into lower states of association when submitted to gel filtration. Isoelectric focusing analysis of the purified enzyme showed a pI of 5.7 and occasionally revealed microheterogeneity. The enzy...
متن کاملThe Interaction of Tetraiodofluorescein with Glutamate Dehydrogenase from Bovine Liver
Reports from various laboratories have dealt with the binding properties of glutamate dehydrogenase from bovine liver (EC 1.4.1.3) (Pantaloni & Dessen, 1969; Huang & Frieden, 1969; Malcolm, 1972; Brown et al., 1973; Koberstein & Sund, 1973), but unfortunately these reports differ considerably over the number and nature of glutamate dehydrogenase coenzyme-binding sites as well as the magnitude o...
متن کاملPurification of Mitochondrial Glutamate Dehydrogenase from Dark-Grown Soybean Seedlings.
Proteins in extracts from cotyledons, hypocotyls, and roots of 5-d-old, dark-grown soybean (Glycine max L. Merr. cv Williams) seedlings were separated by polyacrylamide gel electrophoresis. Three isoforms of glutamate dehydrogenase (GDH) were resolved and visualized in gels stained for GDH activity. Two isoforms with high electrophoretic mobility, GDH1 and GDH2, were in protein extracts from co...
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ژورنال
عنوان ژورنال: Plant Physiology
سال: 1972
ISSN: 0032-0889,1532-2548
DOI: 10.1104/pp.49.1.87