title: The molecular size and shape of the Folch-Pi apoprotein in aqueous and organic solvents.
abstract: In 1% acetic acid, sedimentation velocity measurements and equilibrium ultracentrifuge experiments demonstrate that the Folch-Pi apoprotein is not monodisperse. The weight-average molecular weight calculated from ultracentrifuge experiments and combining sedimentation coefficient and viscosity measurements, ranged from 64000 to 80000. The intrinsic viscosity value suggests an asymetric shape for the apoprotein if a low value of hydration is considered. In dioxan/1% acetic acid (2:3, v/v) a smaller sedimentation coefficient was found, the intrinsic viscosity value remaining identical to that in 4% acetic acid. In pure 2-chloroethanol, light-scattering experiments led to a molecular weight of 165000 indicating that even in this solvent the protein is not monomeric. Intrinsic viscosity and light scattering measurements on the one hand, primary sequence on the other hand (six proline residues per monomer of Mr 23500) suggest that the molecule in 2-chloroethanol may consist of rod-like segments with flexible junctions.
mesh_terms: D000085:Acetates; D001059:Apoproteins; D007700:Kinetics; D008027:Light; D008970:Molecular Weight; D009185:Myelin Proteins; D011487:Protein Conformation; D011510:Proteolipids; D012542:Scattering, Radiation; D014783:Viscosity
chemical_list: D000085:Acetates; D001059:Apoproteins; D009185:Myelin Proteins; D011510:Proteolipids