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Purification of soluble tetrodotoxin-sensitive protein from the cytoplasmic fraction of bovine brain tissue
Authors:M. K. Malysheva  V. K. Lishko  V. A. Zhukareva  V. V. Lysenko  L. A. Tret'yakov
Abstract:Highly purified protein preparations promoting TTX-dependent sodium permeability in the liposomal membrane were separated from the cytoplasmic fraction of bovine brain tissue. The protein was purified using anion-exchange and separation chromatography and gel filtration. The separated protein was found to be a high-molecular acidic glycoprotein forming 55 kD subunits during denaturation under reducing conditions. It was thought to contribute to the formation of voltage-dependent sodium channels in the cell membrane.A. A. Bogomolets Institute of Physiology and A. V. Palladin Institute of Biochemistry, Academy of Sciences of the USSR, Kiev. Translated from Neirofiziologiya, Vol. 19, No. 2, pp. 202–209, March–April, 1987.
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