Abstract
Study of the 14CO 2 output upon incubating d-leucine-1- 14C and valine-1- 14C with rat liver and kidney slices for 10 and 20 min showed that more was produced from them than from their l isomers. In the intact fasted animal, the l-amino acid yielded about as much 14CO 2 in 4 hr as the d-amino acid did. When it was provided as a component of a complete amino acid mixture, it produced markedly less 14CO 2, its d isomer only slightly less. Mitochondrial-peroxisomal fractions of rat kidney tissue yielded more CO 2 from d-leucine-1- 14C than from its l isomer in 20 min of incubation, but still more from their common α-keto analog. The data suggest that inversion of d-leucine and d-valine is begun by d-amino acid oxidase, but reamination of the α-keto intermediate is largely prevented by its oxidative decarboxylation as formed. In the intact animal gastrointestinal and tissue retention and urinary loss appear to be of relatively minor influence.
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