Sources of ammonia for urea synthesis in isolated rat liver cells

l-Leucine inhibits urea synthesis in rat hepatocytes from a number of nitrogen sources, including ammonia. The inhibition by l-leucine is largely overcome by addition of 1 mM l-ornithine, suggesting that the main site of l-leucine action is at ornithine transcarbamylase, rather than at glutamate dyh...

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Published inBiochimica et biophysica acta Vol. 496; no. 2; pp. 249 - 254
Main Author Rognstad, Robert
Format Journal Article
LanguageEnglish
Published Netherlands Elsevier B.V 28.02.1977
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ISSN0304-4165
0006-3002
1872-8006
DOI10.1016/0304-4165(77)90306-3

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Summary:l-Leucine inhibits urea synthesis in rat hepatocytes from a number of nitrogen sources, including ammonia. The inhibition by l-leucine is largely overcome by addition of 1 mM l-ornithine, suggesting that the main site of l-leucine action is at ornithine transcarbamylase, rather than at glutamate dyhydrogenase. l-Norvaline is a more potent inhibitor of urea synthesiss than is l-leucine, but again the inhibition is largely counteracted by l-ornithine. Addition of aminooxyacetate and l-norvaline strongly suppresses the formation of glucose and lactate from l-asparagine, suggesting that an alternate pathway of aspartate metabolism, the purine nucleotide cycle, in not a major pathway. Hadacidin, an inhibitor of adenylosuccinate synthetase, an enzyme of the purine nucleotide cycle, has no effect on urea synthesis in rat liver cells.
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ISSN:0304-4165
0006-3002
1872-8006
DOI:10.1016/0304-4165(77)90306-3