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Subunit Structure of α‐Bungarotoxin Binding Component in Mouse Brain
Author(s) -
Seto Akiko,
Arimatsu Yasuyoshi,
Amano Takehiko
Publication year - 1981
Publication title -
journal of neurochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.75
H-Index - 229
eISSN - 1471-4159
pISSN - 0022-3042
DOI - 10.1111/j.1471-4159.1981.tb05310.x
Subject(s) - bungarotoxin , protein subunit , component (thermodynamics) , neuroscience , chemistry , microbiology and biotechnology , biology , biochemistry , physics , acetylcholine receptor , receptor , thermodynamics , gene
The α‐bungarotoxin binding component in mouse brain was purified by affinity chromatography with toxin‐Sepharose, gel‐chromatography on Sepharose 6B, and ion‐exchange chromatography with DE52 resin. The iodinated product of the last step produced one major and one minor band on sodium dodecyl sulphate‐polyacrylamide gel electrophoresis (SDS‐PAGE). The molecular weight of the minor peak was twice as large as that of the major one. The iodinated product could bind α‐bungarotoxin, and this binding was inhibited by a nicotinic antagonist, d ‐tubocurarine, which demonstrated that the iodinated product was a true α‐bungarotoxin binding component. The molecular structure of the product was analysed by cross‐linking followed by SDS‐PAGE. The results fitted the model for an α‐bungarotoxin binding component in the mouse brain composed of six identical or very similar subunits of 51,000‐52,000. One subunit carrying the binding site for toxin bound one molecule of toxin. This subunit structure of an α‐bungarotoxin binding component in the brain is discussed in comparison with that of a nicotinic acetylcholine receptor in the electric organ.