title: Characterization and partial purification of a neuronal factor which increases acetylcholine receptor aggregation on cultured muscle cells.
abstract: Medium conditioned by NG108-15 neuroblastoma x glioma hybrid cells contains a factor which increases the number of acetylcholine receptor (AChR) aggregates on cultured myotubes. Protease digestion indicates that the AChR aggregation factor is a protein, and the molecular weight is from 150,000 to 250,000 daltons as estimated by ultrafiltration and gel filtration. Preparative isoelectrofocusing indicates that the aggregation factor has a pI of about 4.7. The factor is found in the soluble cytoplasmic fraction but not in the plasma membrane fraction of NG108-15 cells. Aggregation activity is not detected in the cytoplasm of liver cells or in the cytoplasm of C6BU-1 glioma cells. A possible developmental role for the aggregation factor is suggested by its presence in embryonic rat brain but not in adult rat brain. AChR aggregation factors found in the cytoplasm or conditioned medium of NG108-15 cells or in the cytoplasmic fraction of fetal brain have similar molecular weights and isoelectric points.
mesh_terms: D000109:Acetylcholine / Q000378:metabolism*; D000818:Animals; D002460:Cell Line; D005910:Glioma / Q000201:enzymology; D008970:Molecular Weight; D009132:Muscles / Q000201:enzymology*; D009419:Nerve Tissue Proteins / Q000502:physiology*; D009447:Neuroblastoma / Q000201:enzymology; D051381:Rats; D011950:Receptors, Cholinergic / Q000378:metabolism*
chemical_list: D009419:Nerve Tissue Proteins; D011950:Receptors, Cholinergic; D000109:Acetylcholine