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Cited by 203

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

Open access
Beneski, D A, Catterall, W A·1980·Proceedings of the National Academy of Sciences

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.

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Metadata

Authors
Beneski, D. A., & Catterall, W. A.
Venue
Proceedings of the National Academy of Sciences
Published
1980-01
Volume
77
Issue
1
Pages
639-643
ISSN
  • 0027-8424 (ISSN-L)
  • 1091-6490
OpenAlex
W2056464913
Cited by
203
References
0
FWCI
5.93
Type
journal article
Language
en
Open access
green

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CoChat. (2026). Citation check: Covalent labeling of protein components of the sodium channel with a photoactivable derivative of scorpion toxin. https://app.cochat.ai/papers/10.1073/pnas.77.1.639
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Beneski, D. A., & Catterall, W. A. (1980). Covalent labeling of protein components of the sodium channel with a photoactivable derivative of scorpion toxin. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.77.1.639

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Bibliographic data: Semantic Scholar, OpenAlex, Crossref.

Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.