Enzymes of phospholipid biosynthesis in rat alveolar type II cells
SK Hoehn, E Lesperance, DJ Klass - Lung, 1983 - Springer
SK Hoehn, E Lesperance, DJ Klass
Lung, 1983•SpringerSome enzymes responsible for de novo synthesis of phosphatidylcholine and the
reacylation of phosphatidylcholine to disaturated phosphatidylcholine have been examined
in isolated rat type II alveolar cells. Compared to the enzyme levels found in whole lung
homogenate, levels of choline kinase, choline phosphotransferase and lysolecithin
acyltransferase are enriched 10 fold in isolated type II alveolar cells. No enrichment of
cholinephosphate cytidyltransferase was observed suggesting that this enzyme may be rate …
reacylation of phosphatidylcholine to disaturated phosphatidylcholine have been examined
in isolated rat type II alveolar cells. Compared to the enzyme levels found in whole lung
homogenate, levels of choline kinase, choline phosphotransferase and lysolecithin
acyltransferase are enriched 10 fold in isolated type II alveolar cells. No enrichment of
cholinephosphate cytidyltransferase was observed suggesting that this enzyme may be rate …
Abstract
Some enzymes responsible for de novo synthesis of phosphatidylcholine and the reacylation of phosphatidylcholine to disaturated phosphatidylcholine have been examined in isolated rat type II alveolar cells. Compared to the enzyme levels found in whole lung homogenate, levels of choline kinase, choline phosphotransferase and lysolecithin acyltransferase are enriched 10 fold in isolated type II alveolar cells. No enrichment of cholinephosphate cytidyltransferase was observed suggesting that this enzyme may be rate limiting in phosphatidylcholine biosynthesis.
Springer