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Role of N-acetylglutamate turnover in urea synthesis of rats given proteins of different quality. | LitMetric

Role of N-acetylglutamate turnover in urea synthesis of rats given proteins of different quality.

J Nutr Sci Vitaminol (Tokyo)

Laboratory of Nutritional Biochemistry, School of Food and Nutritional Sciences, COE Program in 21st Century, The University of Shizuoka, Shizuoka 422-8526, Japan.

Published: April 2005

AI Article Synopsis

  • The study aimed to investigate the impact of N-acetylglutamate synthesis and degradation on urea production when varying dietary protein quality in rats.
  • Rats were fed diets with different protein sources (gluten, casein, whole egg protein) for ten days, revealing increased urea excretion and liver concentrations of N-acetylglutamate and free glutamate with lower protein quality.
  • Findings indicate that lower quality protein leads to higher N-acetylglutamate synthesis and reduced degradation in the liver, which enhances urea production.

Article Abstract

The purpose of this study was to find whether the synthesis and degradation of N-acetylglutamate would affect urea synthesis when the dietary protein quality was manipulated. Experiments were done on three groups of rats given diets containing 10 g gluten, 10 g casein or 10 g whole egg protein/100 g for 10 d. The urinary excretion of urea, the liver concentrations of N-acetylglutamate and free glutamate, the liver activity of N-acetylglutamate synthetase increased with the decline in quality of dietary protein. A reverse correlation was observed between the liver N-acetylglutamate degradation and liver Nacetylglutamate concentration. N-Acetylglutamate concentration in the liver was closely correlated with the concentration of glutamate and the N-acetylglutamate synthetase activity in the liver, and excretion of urea. These results suggest that the greater synthesis and the lower degradation rate of N-acetylglutamate in the liver of rats given the lower quality of protein increase the liver concentration of N-acetylglutamate and stimulate urea synthesis.

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Source
http://dx.doi.org/10.3177/jnsv.51.93DOI Listing

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