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PMID: 6928649 Published · ppublish English Journal Article Research Support, U.S. Gov't, P.H.S.

Covalent labeling of protein components of the sodium channel with a photoactivable derivative of scorpion toxin.

Proceedings of the National Academy of Sciences of the United States of America ·Vol. 77 ·No. 1 ·1980-01-00 ·Pages 639-43

Beneski DA, Catterall WA

Abstract

Azidonitrobenzoyl mono[125I]iodo scorpion toxin can be covalently attached to its receptor site in electrically excitable neuroblastoma cells or synaptosomes by photolysis. A polypeptide of Mr approximately 250,000 is specifically labeled in neuroblastoma cells. Labeling is blocked by unlabeled scorpion toxin and by depolarization. This polypeptide is not labeled in a variant neuroblastoma clone lacking voltage-sensitive sodium channels. Polypeptides of Mr approximately 250,000 and Mr approximately 32,000 are specifically labeled in synaptosomes. This labeling is also blocked by unlabeled toxin and by depolarization. These results identify specific polypeptides of Mr approximately 250,000 and Mr approximately 32,000 that are components of the sodium channel.

MeSH Terms
Affinity Labels Animals Brain/metabolism Cells, Cultured Ion Channels/drug effects,metabolism Membrane Proteins/metabolism Molecular Weight Neuroblastoma Photochemistry Potassium/pharmacology Rats Scorpion Venoms/antagonists & inhibitors,pharmacology Synaptosomes/metabolism
Chemicals
Affinity Labels Ion Channels Membrane Proteins Scorpion Venoms Potassium
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Beneski D A
Catterall W A
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24 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.77.1.639
Published
1980-01-00
Pages
639-43
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC348330
Subset
IM
External Links
PubMed source DOI: 10.1073/pnas.77.1.639 PMC Full Text View journal details
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