Abstract
The optimal in vivo conditions for measuring liver acyl-CoA:cholesterol acyltransferase, EC.2.2.1.26 (ACAT) activity in cytoplasmic extract from guinea-pigs have been examined. ACAT in liver from ordinarily fed guinea-pigs is very low. The effect of different compounds on ACAT activity was evaluated. Sodium fluoride, oligomycin, divalent cations, oleyl-CoA, and bile acids were all shown to inhibit ACAT activity markedly. Albumin stimulated the cholesterol esterification independently of the presence of fatty acids. Subcellular distribution of liver ACAT in relation to different marker enzymes shows that the bulk of ACAT activity is present in the microsomal fraction. By comparing the esterification of exogenous and endogenous cholesterol, the results indicate that these two substrates are not esterified to the same extent. Both the 'enzyme" level and substrate quality are of importance for the high ACAT activity found in rat-liver homogenates compared to guinea-pig.
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