title: Purification of bovine glia maturation factor and characterization with monoclonal antibody.
abstract: Glia maturation factor (GMF) is purified 100 000-fold to apparent homogeneity from bovine brains by a procedure consisting of ammonium sulfate precipitation, column chromatography with diethylaminoethyl-Sephacel, Sephadex G-75, and hydroxylapatite, and a final step using C4 reverse-phase high-performance liquid chromatography. The product shows a single protein band in sodium dodecyl sulfate-polyacrylamide gel. It has a molecular weight of 14 000 and an isoelectric point of pH 5.2. Purified GMF stimulates cultured astroblasts to proliferate and to grow out cell processes with half-maximal activity at 8 ng/mL. A monoclonal antibody raised against partially purified GMF adsorbs the activity of pure GMF and immunologically binds the putative GMF protein band.
mesh_terms: D000596:Amino Acids / Q000032:analysis; D000818:Animals; D000911:Antibodies, Monoclonal; D001923:Brain Chemistry; D002417:Cattle; D002851:Chromatography, High Pressure Liquid; D004591:Electrophoresis, Polyacrylamide Gel; D004797:Enzyme-Linked Immunosorbent Assay; D020904:Glia Maturation Factor; D006133:Growth Substances / Q000302:isolation & purification*; D051379:Mice; D008807:Mice, Inbred BALB C; D008970:Molecular Weight; D009419:Nerve Tissue Proteins / Q000276:immunology / Q000302:isolation & purification*
chemical_list: D000596:Amino Acids; D000911:Antibodies, Monoclonal; D020904:Glia Maturation Factor; D006133:Growth Substances; D009419:Nerve Tissue Proteins