Abstract
The activities of pyruvate carboxylase and of pyruvate dehydrogenase in intact rat liver mitochondria were measured under various experimental conditions. In agreement with previous findings, the pyruvate dehydrogenase activity was found to be strongly inhibited by octanoate and palmitoyl-carnitine. Pyruvate carboxylase activity was not altered in the presence of octanoate, when high concentrations of pyruvate were used. However, with low concentrations of pyruvate, octanoate and palmitoyl-carnitine stimulated the carboxylation of pyruvate by 53% and 61% respectively.
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