Studies on the lecithin: cholesterol acyltransferase substrate properties of HDL as determined by its subclass distribution analysed by gradient gel electrophoresis.

Journal article

In order to study the impact of high-density lipoproteins (HDL) subclasses on the ability of HDL to act as substrate for lecithin: cholesterol acyltransferase (LCAT), we isolated HDL from nine normolipidemic male subjects. The HDL particle size distribution was analysed by gradient gel electrophoresis and the esterification rate of the isolated homologous HDL was compared with a pool of HDL where all the nine subjects took part. It was found that the strongest determinant for HDL cholesterol esterification rate was the inhibitory action of HDL subclass 2B.

Authors: Karpe, F; Johansson, J; Carlson, L

• Publication status: Published
• Journal: Biochimica et biophysica acta
• Volume: 1042
• Issue: 3
• Pages: 310-314
• Publication date: 1990-02-01
• DOI: 10.1016/0005-2760(90)90158-t
• ISSN: 0006-3002
• Language: English
• Keywords: Fasting; Cholesterol Esters; Lipoproteins, HDL; Dietary Fats; Electrophoresis, Polyacrylamide Gel; Substrate Specificity; Lipids; Male; Adult; Cholesterol, HDL; Humans; Phosphatidylcholine-Sterol O-Acyltransferase