Preparation and properties of vesicles of a purified myelin hydrophobic protein and phospholipid. A spin label study.
Lipophilin, a hydrophobic protein purified from the proteolipid of normal hupid and protein in 2-chloro-ethanol followed by dialysis against buffer. This method resulted in homogeneous incorporation of the protein into lipid vesicles as judged by sedimentation on a sucrose gradient and freeze fracture electreter and the freeze fracture faces contained intramembrane particles. The effect of lipophilin on the organization of the lipid was studied by use of spin label probes. Two distinct components were present in the spectrum of fatty acid spin labels in the lipid-protein vesicles. One was immobilized presumably due to the presence of boundary lipid around the protein and the second component waicles and probably due to a lamellar phase but with a slightly greater order parameter. Lipophilin was found to increase the order parameter linearly with increasing concentration of protein incorporated into the vesicles. However, the phase transition temperature as measured from the 2,2,6,6-tetramethyl piperidine-1-oxyl (TEMPO) solubility parameter was unchanged.
D001921:Brain; D004578:Electron Spin Resonance Spectroscopy; D005614:Freeze Fracturing; D006801:Humans; D007700:Kinetics; D008567:Membranes, Artificial; D008854:Microscopy, Electron; D008954:Models, Biological; D008968:Molecular Conformation; D009185:Myelin Proteins; D010713:Phosphatidylcholines; D011485:Protein Binding; D011487:Protein Conformation; D013113:Spin Labels; D013696:Temperature; D013816:Thermodynamics
D008567:Membranes, Artificial; D009185:Myelin Proteins; D010713:Phosphatidylcholines; D013113:Spin Labels