title: Semlike Forest virus membrane proteins. Preparation and characterization of spike complexes soluble in detergent-free medium.
abstract: After Triton X-100 delipidation and subsequent Triton X-100 removal in a sucrose gradient the membrane protein spikes of Semliki Forest virus remained soluble in aqueous buffers. It was shown they were present as octameric complexes with a molecular weight of 95-10(4) and that they contain less than 4% lipid and detergent by weight. In electron microscopy after negative staining they appeared as "rosette"-shaped particles. Part of the protein could also be found associated in ordered paracrystalline arrays.
mesh_terms: D003460:Crystallization; D004591:Electrophoresis, Polyacrylamide Gel; D046911:Macromolecular Substances; D008566:Membranes / Q000648:ultrastructure; D008854:Microscopy, Electron; D008970:Molecular Weight; D011092:Polyethylene Glycols; D011485:Protein Binding; D011487:Protein Conformation; D012672:Semliki forest virus / Q000648:ultrastructure*; D014764:Viral Proteins / Q000302:isolation & purification
chemical_list: D046911:Macromolecular Substances; D014764:Viral Proteins; D011092:Polyethylene Glycols