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On the capacity of the β‐oxidation of palmitate and palmitoyl‐esters in rat liver mitochondria

1978; Wiley; Volume: 104; Issue: 3 Linguagem: Inglês

10.1111/j.1748-1716.1978.tb06285.x

1365-201X

Mikael Farstad, Rolf K. Berge,

Adipose Tissue and Metabolism

The beta-oxidation of palmitate, palmitoyl-CoA and palmitoyl-L-carnitine proceeded at a high rate in isolated rat liver mitochondria. At high concentrations (100 nmol/mg protein) the oxidation of palmitate and palmitoyl-CoA was only partly carnitine dependent. All substrates were most rapidly oxidized in the presence of oxaloacetate and state 3 conditions. Succinate inhibited beta-oxidation especially in state 4 conditions. beta-Oxidation was faster in hypotonic than in isotonic medium both in state 3 and state 4 conditions. Hypertonicity inhibited beta-oxidation. The initial formation of palmitoyl-CoA from palmitate, CoA and ATP was faster than the oxidation of palmitate under identical conditions. The presence of bovine serum albumin inhibited the beta-oxidation, especially with palmitoyl-CoA or free palmitate as the substrates. Mitochondria contain a palmitoyl-CoA hydrolase which may influence the available intramitochondrial palmitoyl-CoA. The present results demonstrate no single rate limiting step in the beta-oxidation in vitro. Both the NADH/NAD ratio, competition for the respiratory chain, the level of ADP, binding of palmitoyl-CoA to extramitochondrial protein, and possibly intramitochondrial hydrolysis of palmitoyl-CoA all seem to influence the rate of beta-oxidation in vitro. It is suggested that in vivo the most important factor is the availability of acyl-CoA to the outer carnitine palmitoyl-transferase of the mitochondria.