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Purification and characterization of an. alpha. -bungarotoxin receptor that forms a functional nicotinic channel

Journal Article · · Proceedings of the National Academy of Sciences of the United States of America; (United States)
; ; ;  [1]; ;  [2]
  1. Univ. of Milan (Italy)
  2. Univ. of Duesseldorf (West Germany)

Neither the structure nor the function of {alpha}-bungarotoxin ({alpha}Bgtx) binding molecules in the nervous system have yet been completely defined, although it is known that some of these molecules are related to cation channels and some are not. Using an improved method of affinity chromatography, the authors have isolated a toxin binding molecule from chicken optic lobe that contains at least three subunits with apparent M{sub r} values of 52,000, 57,000, and 67,000. The M{sub r} 57,000 subunit binds {alpha}Bgtx receptors of human neuroblastoma cells, fetal calf muscle, and chicken optic lobe but not by antibodies raised against Torpedo acetylcholine receptor, the serum of myasthenic patients, or monoclonal antibody 35. {sup 125}I-labeled {alpha}Bgtx binding to the isolated receptor is blocked, with the same potency, by nicotinic agonists and antagonists, such as nicotine, neuronal bungarotoxin and, d-tubocurarine. When reconstituted in a planar lipid bilayer, the purified {alpha}Bgtx receptor forms cationic channels with a conductance of 50 pS. These channels are activated in a dose-dependent manner by carbamylcholine and blocked by d-tubocurarine.

OSTI ID:
5934269
Journal Information:
Proceedings of the National Academy of Sciences of the United States of America; (United States), Journal Name: Proceedings of the National Academy of Sciences of the United States of America; (United States) Vol. 88:8; ISSN 0027-8424; ISSN PNASA
Country of Publication:
United States
Language:
English

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