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 in | Biochimica et biophysica acta Vol. 496; no. 2; pp. 249 - 254 |
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Main Author | |
Format | Journal Article |
Language | English |
Published |
Netherlands
Elsevier B.V
28.02.1977
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Subjects | |
Online Access | Get full text |
ISSN | 0304-4165 0006-3002 1872-8006 |
DOI | 10.1016/0304-4165(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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Bibliography: | ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 |
ISSN: | 0304-4165 0006-3002 1872-8006 |
DOI: | 10.1016/0304-4165(77)90306-3 |