Abstract
Cholesterol esterification has been measured in rat liver subcellular fractions, using [7–3H] cholesterol, 2–[1–14C oleoyl]-sn-phosphatidylcholine and [1–14C] palmitoyl CoA as substrates. The isolated Golgi apparatus had significant fatty acyl CoA-cholesteryl acyltransferase activity with an optimum at pH 5.8. Cholesteryl esters formed in vitro were predominantly associated with Golgi VLDL particles. The results emphasize the importance of the Golgi apparatus in the assembly of lipoproteins.