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

Henry J. Pownall, W. Barry van Winkle, Quein Pao, Michael Rohde, Antonio M. Gotto

Research output: Contribution to journalArticle

38 Scopus citations

Abstract

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.

Original languageEnglish (US)
Pages (from-to)494-503
Number of pages10
JournalBiochimica et Biophysica Acta (BBA)/Lipids and Lipid Metabolism
Volume713
Issue number3
DOIs
StatePublished - Dec 13 1982

Keywords

  • Apoliprotein A-I
  • cholesterol acyltransferase
  • HDL
  • Lecithin
  • Lipoprotein
  • Lipoprotein model

ASJC Scopus subject areas

  • Endocrinology
  • Biophysics
  • Biochemistry
  • Medicine(all)

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