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α‐TOXIN BINDING PROTEINS IN THE ELECTRIC ORGAN OF TORPEDO MARMORATA STUDIED BY IMMUNOCHEMICAL METHODS
Author(s) -
Mattsson C.,
Heilbronn E.,
Ramlau J.,
Bock E.
Publication year - 1979
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.1471-4159.1979.tb00352.x
Subject(s) - torpedo , neurotoxin , nicotinic acetylcholine receptor , acetylcholine receptor , electric organ , chemistry , membrane , antibody , biochemistry , immunoelectrophoresis , receptor , biology , immunology
— —Crossed immunoelectrophoretic techniques were developed to study the efficiency of the various purification steps in the isolation of nicotinic acetylcholine receptor (nAChR) from Torpedo mormorata electric organ. A new α‐neurotoxin binding assay based on immunoelectrophoresis is also presented. In crude extracts of Torpedo electric organ membranes one type of receptor molecule (M ñ; 300 , 000) was found; an earlier described higher molecular form was shown to be an artifact of affinity chromatography. Polyvalent antibodies against Torpedo electroplaque membranes, antibodies against purified membrane proteins and against Naja naja siamensis α‐neurotoxin revealed four α‐neurotoxin binding antigens (including nAChR). Two of these, nAChR and T 2 , were specific for electroplaque membrane and showed partial immunoidentity but different biochemical and physical properties.