[Purification of a soluble tetrodotoxin-sensitive protein from the cytoplasmic fraction of bovine brain tissue].
作者信息
Malysheva M K, Lishko V K, Zhukareva V A, Lysenko V V, Tret'iakov L A
出版信息
Neirofiziologiia. 1987;19(2):202-9.
PMID:2439928
Abstract
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.
摘要
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