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Cited by 356

The DOI matches its Crossref record; 19 of the 19 references it cites were found in a registry or an index.

The sodium channel from rat brain. Purification and subunit composition.

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Hartshorne, R P, Catterall, W A·1984·Journal of Biological Chemistry

Abstract

A procedure is described for purification of the sodium channel 1380-fold from rat brain to essential homogeneity. The channel is solubilized in Triton X-100 and stabilized by addition of phosphatidylcholine and 10 mM CaCl2. It is purified by sequential chromatography on DEAE-Sephadex, hydroxylapatite, and wheat germ agglutinin/Sepharose followed by sedimentation through sucrose gradients. The final preparation binds 2910 pmol of saxitoxin (STX)/mg of protein or 0.9 mol of STX/mol of sodium channel of Mr approximately 316,000. Three polypeptide subunits comprise 90% of the silver stain intensity on sodium dodecyl sulfatepolyacrylamide gels of the pure protein and migrate as a stoichiometric complex coincident with STX-binding activity in sucrose gradient sedimentation: alpha with Mr approximately 260,000, beta 1 with Mr approximately 39,000, and beta 2 with Mr approximately 37,000. The alpha subunit, both purified and in intact synaptosomes, is shown to behave anomalously during sodium dodecyl sulfate-polyacrylamide gel electrophoresis exhibiting an unusually high extrapolated electrophoretic free mobility. A subunit stoichiometry of alpha 1(beta 1)1(beta 2)1 is proposed.

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Metadata

Authors
Hartshorne, R. P., & Catterall, W. A.
Venue
Journal of Biological Chemistry
Publisher
Elsevier BV
Published
1984-02
Volume
259
Issue
3
Pages
1667-1675
ISSN
0021-9258 (ISSN-L)
OpenAlex
W1653329430
Cited by
356
References
19
FWCI
12.20
Type
journal article
Language
en
Open access
hybrid

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CoChat. (2026). Citation check: The sodium channel from rat brain. Purification and subunit composition. https://app.cochat.ai/papers/10.1016/s0021-9258(17)43460-0
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Hartshorne, R. P., & Catterall, W. A. (1984). The sodium channel from rat brain. Purification and subunit composition. Journal of Biological Chemistry. https://doi.org/10.1016/s0021-9258(17)43460-0

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