Abstract
A study of respiration of the liver mitochondria of rats after 48 h of starvation revealed a fall of 20% in the rate of ADP-stimulated substrate oxidation compared with the rate of uncoupled respiration. This effect was abolished by preincubation of the mitochondria with carnitine. In the case of liver mitochondria from satiated rats there was a marked decrease in the rate of respiration both in state 3 and in state 4, which was not abolished by carnitine. Preincubation of these mitochondria with α-ketoglutarate led to an increase in the rate of respiration in states 3 and 4 during succinate oxidation. The results suggest the existence of at least two methods of regulation of adenine-nucleotide transport in the mitochondrion depending on the metabolic state of the organism: 1) inhibition of adenine-nucleotide translocase by cytoplasmic acyl-CoA; 2) control of the state of the endogenous adenine-nucleotide reserves in the mitochondrion.
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