| pubmed-article:6319405 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:6319405 | lifeskim:mentions | umls-concept:C1882598 | lld:lifeskim |
| pubmed-article:6319405 | lifeskim:mentions | umls-concept:C0037492 | lld:lifeskim |
| pubmed-article:6319405 | lifeskim:mentions | umls-concept:C0486616 | lld:lifeskim |
| pubmed-article:6319405 | lifeskim:mentions | umls-concept:C1998793 | lld:lifeskim |
| pubmed-article:6319405 | lifeskim:mentions | umls-concept:C1711351 | lld:lifeskim |
| pubmed-article:6319405 | pubmed:issue | 3 | lld:pubmed |
| pubmed-article:6319405 | pubmed:dateCreated | 1984-3-16 | lld:pubmed |
| pubmed-article:6319405 | pubmed:abstractText | 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. | lld:pubmed |
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| pubmed-article:6319405 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:6319405 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:6319405 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:6319405 | pubmed:month | Feb | lld:pubmed |
| pubmed-article:6319405 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:6319405 | pubmed:author | pubmed-author:CatterallW... | lld:pubmed |
| pubmed-article:6319405 | pubmed:author | pubmed-author:HartshorneR... | lld:pubmed |
| pubmed-article:6319405 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:6319405 | pubmed:day | 10 | lld:pubmed |
| pubmed-article:6319405 | pubmed:volume | 259 | lld:pubmed |
| pubmed-article:6319405 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:6319405 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:6319405 | pubmed:pagination | 1667-75 | lld:pubmed |
| pubmed-article:6319405 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
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| pubmed-article:6319405 | pubmed:year | 1984 | lld:pubmed |
| pubmed-article:6319405 | pubmed:articleTitle | The sodium channel from rat brain. Purification and subunit composition. | lld:pubmed |
| pubmed-article:6319405 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:6319405 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:6319405 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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