Physical Properties of the Dimyristoylphosphatidylcholine Vesicle and of Complexes Formed by Its Interaction with Apolipoprotein C-III

Kirk C. Aune, Joseph G. Gallagher, Antonio M. Gotto, Joel D. Morrisett

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41 Scopus citations

Abstract

The structure of a single bilayer vesicle of dimyristoylphosphatidylcholine has been characterized by sedimentation, densimetry, and light-scattering measurements. The molecular weight, partial specific volume, Stokes radius, and degree of hydration were found to be 2.68 ∓ 106, 0.972 cm3/g, 125 Å, and 0.86 g/g, respectively. From these quantities, a spherically symmetrical model has been derived that features a phospholipid bilayer 35.5 A thick and a hydration shell 9.3 A thick. This particle was shown to bind 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 molecular weight. 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 molecular weight were found to be ∼80 Å and 442 000, respectively. Within the constraints of these values and other data, several models for this complex are discussed.

Original languageEnglish (US)
Pages (from-to)2151-2156
Number of pages6
JournalBiochemistry
Volume16
Issue number10
DOIs
StatePublished - May 1 1977

ASJC Scopus subject areas

  • Biochemistry

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