Purification of soluble tetrodotoxin-sensitive protein from the cytoplasmic fraction of bovine brain tissue View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

1987-03

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. More... »

PAGES

157-163

Identifiers

URI

http://scigraph.springernature.com/pub.10.1007/bf01056808

DOI

http://dx.doi.org/10.1007/bf01056808

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1016343624


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