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  • Title: Comparison of ACYL-CoA : lysophosphatidylcholine acyltransferase and lysophosphatidylcholine : lysophosphatidylcholine transacylase activity in various mammalian lungs.
    Author: Van Heusden GP, Van den Bosch H.
    Journal: Biochim Biophys Acta; 1981 Dec 23; 666(3):508-11. PubMed ID: 7326258.
    Abstract:
    Lung disaturated phosphatidylcholine is thought to by synthesized, at least partially, by remodelling of unsaturated phosphatidylcholines. In view of the putative role of acyl-CoA : lysophosphatidylcholine acyltransferase (EC 2.3.1.23) and lysophosphatidylcholine : lysophosphatidylcholine transacylase in this remodelling process the activity of these enzymes in the lung of various mammals was investigated. The acyl-CoA-dependent acylation pathway was easily detected in the microsomal fractions of all animals investigated. By contrast, the enzyme catalyzing a transacylation between two molecules of lysophosphatidylcholine was only present in the 100 000 X g supernatants of rat, rabbit and mouse lung. It appeared to be undetectable in these fractions from guinea pig, bovine, pig, horse and sheep lung. These results provide and additional argument for the idea that the transacylation does not contribute to the synthesis of dipalmitoyl phosphatidylcholine in vivo.
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