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- W1882970239 abstract "1. l-Leucine strongly activated intramitochondrial glutamate dehydrogenase in the direction of glutamate synthesis. 2. In the deamination direction, the enzyme was not stimulated by leucine. This was probably due to a rate-limiting transport of glutamate across the mitochondrial membrane. 3. The effect of leucine on the kinetic constants of glutamate dehydrogenase in a mitochondrial sonicate was studied. 4. In isolated mitochondria, leucine did not stimulate the synthesis of citrulline with glutamate as the source of NH3. 5. Leucine very markedly stimulated the synthesis of glutamate from added 2-oxoglutarate+NH4Cl. 6. Under conditions where glutamate and citrulline could be synthesized simultaneously from added NH4Cl, leucine greatly increased glutamate synthesis at the expense of citrulline synthesis. 7. It is suggested that the intramitochondrial leucine concentration may be a factor influencing the nitrogen metabolism of the liver cell." @default.
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- W1882970239 date "1973-05-15" @default.
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- W1882970239 title "Effect of <scp>l</scp>-leucine on the nitrogen metabolism of isolated rat liver mitochondria" @default.
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- W1882970239 doi "https://doi.org/10.1042/bj1340209" @default.
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