In vitro polymerization of glial fibrillary acidic (GFA) protein extracted from multiple sclerosis (MS) brain.
Aqueous extracts of multiple sclerosis plaques were used for reaggregation studies of filamentous proteins. Filament formation as observed by electron microscopy was dependent on temperature, pH, and energy. The major protein component in the filaments had chemical and immunological properties of the glial fibrillary acidic protein.
D001923:Brain Chemistry; D055598:Chemical Phenomena; D002621:Chemistry; D004591:Electrophoresis, Polyacrylamide Gel; D005904:Glial Fibrillary Acidic Protein; D006160:Guanosine Triphosphate; D006801:Humans; D005779:Immunodiffusion; D046911:Macromolecular Substances; D008854:Microscopy, Electron; D008970:Molecular Weight; D009103:Multiple Sclerosis / Q000378:metabolism*; D009419:Nerve Tissue Proteins / Q000302:isolation & purification / Q000378:metabolism*; D009457:Neuroglia / Q000032:analysis; D011863:Radioimmunoassay / Q000379:methods
D005904:Glial Fibrillary Acidic Protein; D046911:Macromolecular Substances; D009419:Nerve Tissue Proteins; D006160:Guanosine Triphosphate