MechanismsLandmark
The original isolation of the 74kDa human plasma CETP reveals a leucine-rich, highly hydrophobic protein specific for cholesteryl ester over triglyceride transfer (Proc Natl Acad Sci U S A 1987)
Original title: Isolation and specificity of a Mr 74,000 cholesteryl ester transfer protein from human plasma
The authors isolated a cholesteryl ester transfer protein from human plasma whose ligand specificity, molecular weight and amino acid composition differed significantly from proteins previously reported to have this activity. Purified about 100,000-fold from plasma, the protein is rich in hydrophobic amino acids, especially leucine, with a molecular weight of 74,000 and an isoelectric point of 5.2. Its transfer rate for cholesteryl ester was similar between each major plasma lipoprotein class and rapid compared with triacylglycerol transfer, regardless of the donor and acceptor lipoproteins' overall lipid composition. The authors conclude this protein functions primarily in transferring cholesteryl esters between plasma lipoproteins.
Original abstract
A cholesteryl ester transfer protein was isolated from human plasma whose ligand specificity, molecular weight, and amino acid composition are significantly different from those of proteins previously reported to have this activity. The protein, purified about 100,000-fold from plasma, is rich in hydrophobic amino acids, especially leucine. It has a molecular weight of 74,000 and an isoelectric point of 5.2. The protein's transfer rate for cholesteryl ester between each of the major plasma lipoprotein classes is similar, and rapid compared to the transfer of triacyglycerol, regardless of the overall lipid composition of the donor and acceptor lipoprotein. These data suggest that this protein functions primarily in the transfer of cholesteryl esters between plasma lipoproteins.
Summary written by cetpinhibition.org from the published abstract; figures as published. Page updated 19 August 2026. Methods.