Rat hepatocyte plasma membrane acyl:CoA synthetase activity

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Abstract
The presence of long chain acyl:CoA synthetases in mammalian microsomes and mitochondria has been established previously by Aas (Biochim. Biophys. Acta 231, 32–47 [1971]). The presence of a plasma membrane-associated enzyme was investigated in rat hepatocyte plasma membranes, where an enzyme exhibiting high activity and with a preferred substrate of 18-carbon chain length was discovered. The results are consistent with the presence of a single enzyme. The effect of the degree of unsaturation of the fatty acid substrates was not as pronounced as that arising from the length of the carbon chain. The pattern of substrate preference of the enzyme was ω3 polyenoic fatty acids >ω6 polyenoic acids >ω9 monoenoic acids > saturated acids. This may relate to the similar substrate preference pattern exhibited by the fatty acyl desaturase enzymes. The role played by long chain acyl:CoA synthetase in hepatocyte metabolism is uncertain, but it may relate to the incorporation of polyenoic fatty acids from the circulation into cell membranes and the trapping of other fatty acids within the cell for further metabolism.

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