[Nitrogen detoxification in artificially-fed zinc-deficient rats].
The aim of this investigation was to determine if the hyperammonaemia shown in previous zinc-deficiency experiments was the result of disturbed enzyme activities for urea synthesis caused by zinc deficiency per se or was a secondary effect of the reduced feed intake accompanying energy and protein deficiency. For this, 24 male Sprague-Dawley rats with an average body weight of 109 g were divided into two groups of 12 animals each. Both groups were force fed by intragastric tube four times daily over 11 experimental days. Group 1 received a zinc-deficient diet (1.3 mg Zn/kg diet) in a total amount of 11.6 g/day/animal. Group 2 received the zinc sulphate-supplemented control diet (25 mg Zn/kg diet) in the same amount. This technique made it possible to supply even the zinc-deficient rats with sufficient nutrients over the whole experimental period in the same manner as for the control rats, at the same time and with the same dietary amounts. At the end of the experiment, the serum zinc concentration and the alkaline phosphatase activity were significantly reduced in the zinc-deficient rats by 59 and 37%, respectively, in comparison with control animals. This showed a severe alimentary zinc-deficiency status of the animals. The concentrations of ammonia and urea, as well as the activity of glutamate dehydrogenase in serum, were not influenced by the zinc-deficient nutrition within the experimental time. Likewise, the mitochondrial activities of glutamate dehydrogenase and carbamoylphosphate synthetase in the liver were not affected by the alimentary zinc concentration. On the contrary, the activities of ornithine carbamoyltransferase and cytosolic liver enzymes argininosuccinate synthetase, argininosuccinase and arginase were significantly increased in comparison with control rats. In the case of a sufficient supply of nutrients, alimentary zinc deficiency did not cause hyperammonaemia owing to disturbed urea synthesis, as previously hypothesized.
Roth
V H
VH
Lehrstuhl für Ernährungsphysiologie, Department für Lebensmittel und Ernährung der Technischen Universität München, D-85350 Freising-Weihenstephan, Deutschland.
D000469:Alkaline Phosphatase / Q000378:metabolism; D000641:Ammonia / Q000097:blood*; D000818:Animals; D001119:Arginase / Q000378:metabolism; D001123:Argininosuccinate Lyase / Q000378:metabolism; D001124:Argininosuccinate Synthase / Q000378:metabolism; D002222:Carbamoyl-Phosphate Synthase (Ammonia) / Q000378:metabolism; D004195:Disease Models, Animal; D004750:Enteral Nutrition / Q000662:veterinary; D005969:Glutamate Dehydrogenase / Q000378:metabolism; D007441:Intubation, Gastrointestinal / Q000662:veterinary; D008099:Liver / Q000201:enzymology; D008297:Male; D009954:Ornithine Carbamoyltransferase / Q000378:metabolism; D051381:Rats; D017207:Rats, Sprague-Dawley; D014508:Urea / Q000097:blood; D015032:Zinc / Q000097:blood / Q000172:deficiency*; D019287:Zinc Sulfate / Q000008:administration & dosage*
D000641:Ammonia; D019287:Zinc Sulfate; D014508:Urea; D005969:Glutamate Dehydrogenase; D009954:Ornithine Carbamoyltransferase; D000469:Alkaline Phosphatase; D001119:Arginase; D001123:Argininosuccinate Lyase; D002222:Carbamoyl-Phosphate Synthase (Ammonia); D001124:Argininosuccinate Synthase; D015032:Zinc