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PMID: 4531016 Published · ppublish English Journal Article Research Support, U.S. Gov't, P.H.S.

Purified acetylcholine receptor: its reconstitution to a chemically excitable membrane.

Proceedings of the National Academy of Sciences of the United States of America ·Vol. 71 ·No. 12 ·1974-12-00 ·Pages 4768-72

Michaelson DM, Raftery MA

Abstract

Association of purified acetylcholine receptor from Torpedo californica electroplax with lipids from the same organism results in a vesicular membrane system in which the receptor protein is oriented so that all neurotoxin binding sites appear to be on the outer surface. The reconstituted system is chemically excitable by acetylcholine and carbamylcholine, as measured by (22)Na(+) efflux. This excitability is specifically blocked by the antagonist alpha-bungarotoxin. These results demonstrate that the purified receptor macromolecule contains not only the specific neurotransmitter binding site but also the molecular elements necessary for ion translocation in order to effect postsynaptic depolarization.

MeSH Terms
Animals Bungarotoxins/metabolism Carbachol/metabolism Centrifugation, Density Gradient Electric Organ/metabolism Fishes Iodine Radioisotopes Lipids Membranes, Artificial Nerve Tissue Proteins/isolation & purification Osmosis Protein Binding Radioisotopes Receptors, Cholinergic Sodium/metabolism Sodium Isotopes
Chemicals
Bungarotoxins Iodine Radioisotopes Lipids Membranes, Artificial Nerve Tissue Proteins Radioisotopes Receptors, Cholinergic Sodium Isotopes Carbachol Sodium
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Michaelson D M
Raftery M A
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26 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.71.12.4768
Published
1974-12-00
Pages
4768-72
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC433978
Subset
IM
External Links
PubMed source DOI: 10.1073/pnas.71.12.4768 PMC Full Text View journal details
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