1. The specific activity of lysolecithin acyltransferase (EC 2.3. 1.23) in sonicated adult rat lung alveolar type II epithelial cells, measured either alone or in combination with acyl-CoA synthetase (EC 6.2. 1.3), was found to be an order of magnitude greater than that of lysolecithin: lysolecithin acyltransferase. 2. Lysolecithin acyltransferase in type II cells was found to prefer palmitoyl-CoA over oleoyl-CoA as substrate. The combination of lysolecithin acyltransferase and acyl-CoA synthetase was found to prefer palmitate over oleate for incorporation into phosphatidylcholine. 3. Compared to whole lung homogenate, sonicated adult rat type II cells are highly enriched in lysolecithin acyltransferase but not in lysolecithin: lysolecithin acyltransferase. 4. These observations indicate that in normal adult rat type II cells the deacylation-reacylation cycle is more important for the formation of dipalmitoyl phosphatidylcholine than the deacylation-transacylation process.