Biomedical subjects

E Rybosová

Publications and source records attributed to E Rybosová.

4 recordsLinked to original sources

PubMed1991

[Glutamate dehydrogenase and glutamine synthetase activity in the digestive tract in lambs in relation to age].

Developmental dynamics was investigated in the activity of glutamate dehydrogenase (GDH, E.C. 1.4.1.2.-4) and glutamine synthetase (GS, E.C. 6.3.1.2) in different parts of the digestive tract of lambs, in dependence on the age from 10 to 90 days; the goal of these investigations was to elucidate in greater detail the role of the above enzymes in nitrogen metabolism. The activity of GDH, and of the coenzymes NADH and NADPH, was followed in the digesta because simple organisms (bacteria, fungi, plants) have two glutamate dehydrogenases: they differ from each other by coenzyme specificity, unlike GDH from animal sources which can utilize both NADH coenzyme and NADPH coenzyme (Fahien et al., 1965; Frieden, 1964). The following activities of GDH and GS were found out in trials with lambs at the age of 10, 20, 30, 40 and 90 days, as to the different parts of digestive tract: in the tissues of rumen, omasum, reticulum, spleen, duodenum, jejunum, ileum, int. caecum and colon the activity of GDH (NADH) varied from 0.031 to 0.305 nkat/mg dry matter, in the digesta from 0 to 2.92 nkat/mg dry matter. An investigation of GDH (NADH, NADPH) dynamics in the digesta of lambs showed the relatively high activity of GDH (NADH) in the digesta of colon at the age of 10 days and that of GDH (NADPH) in the digesta of int. caecum. The activity of GDH (NADH) was also found to be high in the digesta of int. caecum at the age of 20 days. In that period the activity of GDH (NADH, NADPH) in the digesta of rumen, omasum and reticulum was zero.(ABSTRACT TRUNCATED AT 250 WORDS)

Animals↗

PubMed1978

[Changes in the distribution of urea in body fluids during growth].

Urea concentration in plasma, muscle, and liver fluids of Wistar rats at the age of 3, 6, and 12 weeks was determined. In rats at the age of 3 weeks urea was cumulated in liver and muscle tissue fluids, in older rats (6 and 12 weeks) in plasma fluid. According to the stated urea distribution in individual age categories, a higher urea transport from tissues to blood is considered to be in rats at the age of 6 and 12 weeks. The urea transport proved to be one of the mechanisms of facilitating better utilization of endogenous urea nitrogen in bio-synthetic processes of the nitrogen metabolism in ruminants as well as in monogastric animals.

Animals↗

PubMed1976

Incorporation of intravenously administered urea-15N into sheep plasma proteins and their amide groups.

Two sheep with a low and high nitrogen intake (7.6 and 24 g N/day respectively) were given a single intravenous dose of 15N-labelled urea (15.3 mg 15N/kg b.w.) The findings were as follows. The greater part of non-retained 15N from the administered dose was excreted during the first day after the intravenous administration of 15N-urea. Daily excretion in the faeces amounted to 1.35-2.37% of the 15N in the given dose. With a low N intake, more 15N from the given dose (59.4%) was retained in the N pool than with a high N intake (50.5%). The net passage of 15N into the rumen and 15N incorporation into the amide-N of the plasma proteins was likewise greater. 15N incorporation into the amide-N of the plasma proteins rose steadily for 3 days. The porportion of amidic 15N in the plasma proteins rose steadily for 3 days. The proportion of amidic 15N in the plasma protein total 15N changed on the second and third day after administering 15N-urea from 8% to 16%, with the maximum at the beginning of the second day. The amount of 15N incorporated into the proteins in 1 litre plasma attained up to 3% of the given dose. It is concluded from the results that the synthesis of amino acids and their amide groups is both a quantitatively and a qualitatively important metabolic route for the reutilization of blood urea nitrogen for protein synthesis in ruminants.

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PubMedDate not supplied

[The characteristics and regulation of glutamate dehydrogenase in strains of Bacteroides ruminicola ssp. ruminicola isolated from the rumen of fallow deer].

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 non-animal 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; this specificity was different from the coenzyme specificity of GDH isolated from the rumen strain B. ruminicola in calves where GDH was found to be specific to the coenzyme NADPH. The effect of increasing concentrations of NADH, 2-oxoglutarate and NH4+ on the enzyme reaction velocity was also investigated and Km was determined for NADH, 2-oxoglutarate and NH4+ (Tab. II). The kinetic properties of GDH isolated from different sources are considerably variable. Michaelis constants for GDH range from 0.003 to 0.125 mmol/dm3 for NADPH (NADH), from 0.95 to 7.4 mmol/dm3 for 2-oxoglutarate, and from 0.25 to 16 mmol/dm3 for NH4+ (Misono et al., 1985). The average value of Km for NH4+ in a mixed rumen population was 33 mmol/dm3 (Erfle et al., 1977).(ABSTRACT TRUNCATED AT 250 WORDS)

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