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. 1978 Jan-Feb;51(1):19–26.

Influence of L-Leucine on Glutamate Dehydrogenase Activity in Isolated Rat Diaphragm 1

George Palaiologos, Philip Felig
PMCID: PMC2595657  PMID: 676348

Abstract

Glutamate dehydrogenase (NAD) activity was measured in liver and diaphragm mitochondria from 48 h fasted rats. Kinetic studies were performed with diaphragm enzyme and the effects of L-leu, ADP and L-ala on the K1m and V1max for NH4+, and α-ketoglutarate were evaluated. L-leucine increases by 2-8 fold the V1max for all three substrates with no significant changes in the K1m. ADP increased by 3-7 fold the V1max for all three substrates and the K1m for NADH and α-ketoglutarate by 1.5-7.0 fold. L-alanine had no effect on either the V1max or the K1m of any substrate. The results suggest that muscle has the capacity to form glutamate through the glutamate dehydrogenase reaction and that L-leucine may stimulate this reaction in muscle.

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Selected References

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