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The Properties and Control of Glutamate-Dehydrogenase Isolated from the Rumen Strain Bacteroides Ruminicola-Ssp Ruminicola in Fallow Deer

HOLOVSKA K, LENARTOVA V, RYBOSOVA E, ORINAK A, STACHOVA M
Veterinarni Medicina 37, 1992, 261-268

Very little information about NH4+ assimilation paths in rumen anaerobic bacteria is available, and the information about wild animals is completely missing. Glutamate dehydrogenase [GDH] isolated from the rumen strain B. ruminicola in fallow deer was purified and its properties were specified after crystalline ammonium sulphate precipitation and gel filtration on Sephadex G-200. The properties of partly purified GDH were specified. One of the first specifications concerning GDH from various sources was to determine its coenzyme specificity. The results of these determinations enabled to draw a general conclusion that GDH from nonanimal sources was specific to only one coenzyme while GDH from animal sources could utilize the two coenzymes (Frieden, 1964). In our study the specificity of GDH isolated from the rumen strain B. ruminicola in fallow deer to the coenzyme NADH (Tab. I) was determined


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