Open AccessLipid-protein interaction in the phosphatidylcholine exchange protein.
Author(s) -
Philippe F. Devaux,
Peter Moonen,
Alain Bienvenüe,
K.W.A. Wirtz
Publication year - 1977
Publication title -
proceedings of the national academy of sciences of the united states of america
Language(s) - English
Resource type - Journals
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.74.5.1807
Subject(s) - phosphatidylcholine , lecithin , chemistry , egg lecithin , biochemistry , nitroxide mediated radical polymerization , organic chemistry , phospholipid , membrane , monomer , radical polymerization , polymer
Incorporation of 2-acyl spin-labeled lecithin into the phosphatidylcholine protein from bovine liver results in an immobilization of the spin-label at the methyl and the carboxyl terminal end of the acyl chain. The nitroxide group on the protein-bound lecithin molecule is not accessible to ascorbate. This suggests that lecithin is buried in a pocket on the protein, which effectively shields the acyl chains from the medium.