MechanismsLandmark
Chromatography, electrophoresis and immunoprecipitation together show apolipoprotein D and CETP are distinct proteins, resolving early confusion about CETP's identity (Biochim Biophys Acta 1981)
Original title: The separation of apolipoprotein D from cholesteryl ester transfer protein
This study addressed whether cholesteryl ester transfer protein (CETP) and apolipoprotein D are identical. The two proteins did not co-purify during hydrophobic and cationic exchange chromatography and were readily separated by molecular sieve chromatography or electrophoresis. Furthermore, precipitating apolipoprotein D with specific antisera did not diminish the transfer activity of lipoprotein-deficient plasma. The authors conclude apolipoprotein D and cholesteryl ester transfer protein have significantly different physicochemical properties.
Original abstract
This study addresses the question of whether cholesteryl ester transfer protein and apolipoprotein D are identical. The data presented show that these two proteins do not co-purify during hydrophobic and cationic exchange chromatography and are readily separated by molecular sieve chromatography or electrophoresis. Furthermore, the precipitation of apolipoprotein D by specific antisera did not diminish the transfer activity of lipoprotein-deficient plasma. We conclude that apolipoprotein D and cholesteryl ester transfer protein have significantly different physicochemical properties.
Summary written by cetpinhibition.org from the published abstract; figures as published. Page updated 19 August 2026. Methods.