Abstract
Acylcoenzyme A:cholesterol acyltransferase (ACAT) has been solubilized from Ehrlich ascites cell microsomes by extraction with 2% Triton X-100. Activity was obtained with the solubilized material after removal of the detergent, and it was enhanced when the extract was incorporated into liposomes. The activity of the reconstituted system was dependent upon the amount of cholesterol present in the liposomes. It reached a maximum when the molar ratio of cholesterol to phospholipid was 0.074 and decreased when larger amounts of cholesterol were added. The increase in ACAT activity appears to be a substrate effect of cholesterol, whereas the reduction at higher cholesterol contents probably is due to changes in the physical properties of the liposomes.
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