Detection of lipid transfer protein activity in rabbit liver perfusate

Cholesteryl ester, triacylglycerol and phospholipid transfer activity was detected in rabbit liver perfusate after 2 h perfusions in situ. Lipoproteins were removed from the perfusate plasma by ultracentrifugation prior to hydrophobic interaction chromatography of the lipoprotein-free perfusate. The hydrophobic protein, eluted with water from a Phenyl-Sepharose column, facilitated the transfer of radiolabelled cholesteryl ester, triacylglycerol and phosphatidylcholine from low-density lipoprotein to high-density lipoprotein during 3 h incubations at 37 degrees C. These results suggest that rabbit plasma lipid transfer protein is produced by the liver.