Physical properties of the dimyristoylphosphatidylcholine vesicle and of complexes formed by its interaction with apolipoprotein C-III
- 1 May 1977
- journal article
- research article
- Published by American Chemical Society (ACS) in Biochemistry
- Vol. 16 (10) , 2151-2156
- https://doi.org/10.1021/bi00629a017
Abstract
The structure of a single bilayer vesicle of dimyristoylphosphatidylcholine was characterized by sedimentation, densimetry and light-scattering measurements. The MW, partial specific volume, Stokes radius and degree of hydration were found to be 2.68 .times. 106, 0.972 cm3/g, 125 .ANG. and 0.86 g/g, respectively. From these quantities, a spherically symmetrical model was derived that features a phospholipid bilayer 35.5 .ANG. thick and a hydration shell 9.3 .ANG. thick. This particle bound [human very low density lipoprotein] apolipoprotein C-III (apoC-III) up to 0.08 g/g without loss of its original vesicular structure. At protein-lipid ratios in excess of 0.08 g/g, sedimentation, gel chromatography and light-scattering measurements indicated a dramatic decrease in Stokes radius and MW. The sedimentation data showed these parameters to become constant at protein-lipid ratios in excess of 0.25 g/g. In this region, the Stokes radius and MW were .apprx. 80 .ANG. and 442,000, respectively. Within the constraints of these values and other data, several models for this complex are discussed.This publication has 1 reference indexed in Scilit:
- Interaction of Apoprotein from Porcine High-Density Lipoprotein with Dimyristoyl Lecithin. 1. The Structure of the ComplexesEuropean Journal of Biochemistry, 1976