Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1984-3-16
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.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
10
pubmed:volume
259
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1667-75
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1984
pubmed:articleTitle
The sodium channel from rat brain. Purification and subunit composition.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't