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PMID: 5274453 Published · ppublish English Journal Article

Use of a snake venom toxin to characterize the cholinergic receptor protein.

Proceedings of the National Academy of Sciences of the United States of America ·Vol. 67 ·No. 3 ·1970-11-00 ·Pages 1241-7

Changeux JP, Kasai M, Lee CY

Abstract

alpha-Bungarotoxin, a polypeptide of mol wt 8000 purified from the venom of Bungarus multicinctus, blocks irreversibly and specifically the excitation by cholinergic agonists on the isolated electroplax and on purified membrane fragments in vitro. The toxin also blocks the in vitro binding of decamethonium to a protein recently isolated from electric tissue. This observation strengthens our earlier conclusion that this protein is the cholinergic receptor macromolecule.

MeSH Terms
Animals Chemoreceptor Cells/drug effects Decamethonium Compounds/pharmacology Eels Electric Organ/drug effects Membranes/drug effects Molecular Weight Parasympathomimetics/antagonists & inhibitors Peptides/isolation & purification Protein Binding/drug effects Snakes Venoms/pharmacology
Chemicals
Decamethonium Compounds Parasympathomimetics Peptides Venoms
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Changeux J P
Kasai M
Lee C Y
References (18)
18 references, click to expand
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Article Info
Journal
Proceedings of the National Academy of Sciences of the United States of America
Abbr.
Proc Natl Acad Sci U S A
ISSN
0027-8424
DOI
10.1073/pnas.67.3.1241
Published
1970-11-00
Pages
1241-7
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC283343
Subset
IM
External Links
PubMed source DOI: 10.1073/pnas.67.3.1241 PMC Full Text View journal details
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