Characterization of acyl-CoA:cholesterol acyltransferase from neonatal chick liver.
Endogenous cholesterol esterification in chick liver microsomes was catalyzed by acyl-CoA:cholesterol acyltransferase using palmitoyl-CoA as substrate. An acyl-CoA hydrolase activity was also found in our microsomal preparations. Acyltransferase activity was stable after microsomes storage at -40 degrees C for 6 weeks and increased linearly with the preincubation time between 0 and 45 min. In our assay conditions, cholesteryl ester formation was linear up to 0.3 mg of microsomal protein in the reaction vial and 10 min of incubation. Maximal activity was found in reactions carried out in the presence of 1-2 mM dithiothreitol and 1.2 mg of bovine serum albumin, while acyl-CoA hydrolase was clearly inhibited by increasing albumin amounts.
D000818:Animals; D002250:Carbon Radioisotopes; D002645:Chickens; D004355:Drug Stability; D007700:Kinetics; D008862:Microsomes, Liver / Q000201:enzymology*; D010171:Palmitoyl Coenzyme A / Q000378:metabolism; D002785:Sterol O-Acyltransferase / Q000378:metabolism*
D002250:Carbon Radioisotopes; D010171:Palmitoyl Coenzyme A; D002785:Sterol O-Acyltransferase