Localization of horseradish peroxidase-alpha-bungarotoxin binding in crustacean axonal membrane vesicles and intact axons.
A conjugate of alpha-bungarotoxin with horseradish peroxidase was used to visualize alpha-bungarotoxin binding sites at the fine structural level in isolated axonal membrane vesicles from lobster walking leg nerve. These plasma membrane vesicles have previously been shown to exhibit saturable binding of [3H]nicotine and [3H]acetylcholine. Binding of the toxin was identified in the axon plasma membrane and could be blocked by pretreatment with excess free alpha-bungaratoxin or d-tubocurarine. Binding sites for alpha-bungarotoxin were identified by the same technique in sections of intact nerve fibers from both lobster and spider crab and were found to be localized primarily in the axolemma rather than in the Schwann cell membrane.
D000109:Acetylcholine / Q000378:metabolism; D000818:Animals; D001369:Axons / Q000378:metabolism*; D001665:Binding Sites; D003386:Brachyura; D002038:Bungarotoxins / Q000378:metabolism*; D002462:Cell Membrane / Q000378:metabolism; D006651:Histocytochemistry; D006735:Horseradish Peroxidase / Q000378:metabolism*; D008121:Nephropidae; D010544:Peroxidases / Q000378:metabolism*; D012583:Schwann Cells / Q000378:metabolism
D002038:Bungarotoxins; D006735:Horseradish Peroxidase; D010544:Peroxidases; D000109:Acetylcholine