Transmembrane orientation of palmitoyl-CoA: lysophosphatidylcholine acyltransferase in microsomes isolated from an alveolar type II cell adenoma and rat liver.

1. The transverse localization of palmitoyl-CoA : lysophosphatidylcholine acyltransferase in the membrane of microsomal vesicles isolated from mouse lung adenomas and rat liver was studied by treating intact and deoxycholate-disrupted microsomes with trypsin and pronase. 2. The latency of mannose-6-phosphatase was preserved during protease treatment, suggesting that membrane integrity was not affected. 3. In adenoma microsomes 35-50% and in liver microsomes 35% of lysophosphatidylcholine acyltransferase activity is accessible to the action of the proteases. Our results suggest that at least a sizable portion of the active center of the enzyme that is responsible for remodeling phospholipids is embedded in the membrane interior. 4. Since enzymes involved in de novo lipid synthesis are reported to be located at the cytoplasmic surface of the microsomal membrane, our results support the notion that in lipid metabolism distinct metabolic pools might exist at opposite sides of the microsomal membrane.