Antigenic differences between a proteolipid and a proteodetergent from Torpedo electroplax having similar cholinergic binding properties.
The nicotinic acetylcholine receptor from Torpedo marmorata was extracted and purified from the electroplax membranes by using both aqueous detergent (proteodetergent) or chloroform-methanol (proteolipid). When studied with a highly sensitive radioimmunoassay, it was found that both proteins do not cross-react immunologically against an antireceptor antiserum prepared with the proteodetergent. Treatment with organic solvents of the electroplax membranes, as well as of the proteodetergent receptor purified by affinity chromatography, impaired the radioimmunoassay. This suggests that the antigenicity has been affected by the change in solvent polarity, even though both proteins have similar binding properties for cholinergic ligands. These findings do not allow a simple immunological comparison between the cholinergic proteodetergent and the proteolipid as previously stated in the literature.
Barkas
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T
Departement de Biochimie, Université de Genéve Ch-1211, Genéve 4, Switzerland.
De Robertis
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E
Harrison
R
R
Lunt
G G
GG