Association of apolipoprotein A-II with egg phosphatidylcholine unilamellar vesicles.

摘要: Interaction of human apolipoprotein A-II (apoA-II) with egg yolk phosphatidylcholine unilamellar vesicles (diameter, 20-26 nm) was studied. ApoA-II bound to the in a saturable manner and displaced by C-III1 (apoC-III1) while apoC-III1 apoA-II, apparent deformation vesicles, as observed electronmicrographs. Free apoA-II that had been from lipid surface readsorbed successively added medium. Disruption vesicular structure occurred less than 3% under experimental conditions. Isothermal binding data were analyzed according reversible equilibrium model. The dissociation constant, Kd, 5.8 X 10(-7) M, maximum level, N, 1.46 amino acid residues per phospholipid for assuming 70% is outer leaflet Kd N values 7.8 M 1.34 leaflet, respectively. All these parameters show good agreement those triglyceride-phospholipid particles approximately same diameter (J. Biol. Chem. (1983) 258, 10073-10082). Thus represent vesicles.