The sodium channel from rat brain. Purification and subunit composition.
作者： R P Hartshorne , W A Catterall
DOI: 10.1016/S0021-9258(17)43460-0
关键词:
摘要: A procedure is described for purification of the sodium channel 1380-fold from rat brain to essential homogeneity. The solubilized in Triton X-100 and stabilized by addition phosphatidylcholine 10 mM CaCl2. It purified sequential chromatography on DEAE-Sephadex, hydroxylapatite, wheat germ agglutinin/Sepharose followed sedimentation through sucrose gradients. final preparation binds 2910 pmol saxitoxin (STX)/mg protein or 0.9 mol STX/mol Mr approximately 316,000. Three polypeptide subunits comprise 90% silver stain intensity dodecyl sulfatepolyacrylamide gels pure migrate as a stoichiometric complex coincident with STX-binding activity gradient sedimentation: alpha 260,000, beta 1 39,000, 2 37,000. subunit, both intact synaptosomes, shown behave anomalously during sulfate-polyacrylamide gel electrophoresis exhibiting an unusually high extrapolated electrophoretic free mobility. subunit stoichiometry 1(beta 1)1(beta 2)1 proposed.
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