[Purification of a soluble tetrodotoxin-sensitive protein from the cytoplasmic fraction of bovine brain tissue].

Highly purified protein inducing tetrodotoxin-dependent Na fluxes in liposomal membrane was obtained from the cytoplasmic fraction of the bovine brain. The protein was purified by anion-exchange chromatography on DEAE-Servacell and wheat germ agglutinin sepharose (WGA) followed by gel filtration on sepharose 4B. It is a high-molecular weight acidic glycoprotein; during denaturation under reducing conditions it forms 55 kD subunits. It is suggested that the tetrodotoxin-sensitive protein could be a soluble intracellular precursor of the voltage-dependent sodium channels.