Action of lecithin:cholesterol acyltransferase on model lipoproteins. Preparation and characterization of model nascent high density lipoprotein

• Published in: Biochimica et biophysica acta Vol. 713; no. 3; p. 494
• Main Authors: Pownall, H J, Van Winkle, W B, Pao, Q, Rohde, M, Gotto, Jr, A M
• Format: Journal Article
• Language: English
• Published: Netherlands 13-12-1982
• Subjects: Apolipoprotein A-I; Apolipoproteins - blood; Apolipoproteins - isolation & purification; Enzyme Activation; Humans; Kinetics; Lipoproteins, HDL - blood; Microscopy, Electron; Molecular Weight; Phosphatidylcholine-Sterol O-Acyltransferase - blood
• ISSN: 0006-3002
• DOI: 10.1016/0005-2760(82)90309-5

Apolipoprotein A-I, the major protein of human plasma high density lipoprotein, is the primary activator of plasma lecithin:cholesterol acyltransferase. In vitro, the association of apolipoprotein A-I with physiological phosphatidylcholines can be catalyzed by mixing the protein and lipid with sodium cholate, which is removed by chromatography. The apolipoprotein A-I/phospholipid complex has the physical properties of an HDL, and when cholesterol is present the complex is a highly reactive substrate in the lecithin:cholesterol acyltransferase-catalyzed reaction. The relative reactivity of this complex compared with a number of other lipid-protein complexes is presented and discussed.