Identification of a cholinergic-specific antigen Chol-1 as a ganglioside.
An antiserum specific for cholinergic terminals was used to identify an antigen conserved between Elasmobranchs and mammals. Immunohistochemistry and a cytotoxicity test were used to assay the binding of antibody to mammalian terminals. Torpedo electric organ gangliosides totally abolished antibody binding. The highest inhibitory activity was associated with a single polysialoganglioside band on TLC plates. Neuraminidase altered the migration of the inhibitory activity on TLC plates. Antibody binding was inhibited by ganglioside fractions derived from chicken and mammalian brains. A summary of those tissues in which the antigen has been detected is presented. The possible function of the antigen is discussed.
D000818:Animals; D000936:Antigen-Antibody Complex; D000941:Antigens / Q000302:isolation & purification*; D002540:Cerebral Cortex / Q000187:drug effects / Q000276:immunology; D002645:Chickens; D002795:Choline O-Acetyltransferase / Q000378:metabolism; D002855:Chromatography, Thin Layer; D003602:Cytotoxicity, Immunologic; D004557:Electric Organ / Q000032:analysis; D005455:Fluorescent Antibody Technique; D005732:Gangliosides / Q000302:isolation & purification* / Q000494:pharmacology; D006168:Guinea Pigs; D006624:Hippocampus / Q000166:cytology; D007106:Immune Sera; D051381:Rats; D013574:Synaptosomes / Q000187:drug effects / Q000276:immunology; D014101:Torpedo
D000936:Antigen-Antibody Complex; D000941:Antigens; D005732:Gangliosides; D007106:Immune Sera; D002795:Choline O-Acetyltransferase