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Monoclonal antibodies against the native or denatured forms of muscarinic acetylcholine receptors.
Author(s) -
André C.,
Guillet J.G.,
De Backer J.P.,
Vanderheyden P.,
Hoebeke J.,
Strosberg A.D.
Publication year - 1984
Publication title -
the embo journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.484
H-Index - 392
eISSN - 1460-2075
pISSN - 0261-4189
DOI - 10.1002/j.1460-2075.1984.tb01755.x
Subject(s) - muscarinic acetylcholine receptor , monoclonal antibody , acetylcholine receptor , biology , microbiology and biotechnology , receptor , antibody , biochemistry , immunology
BALB/c mice were immunized with affinity‐purified muscarinic acetylcholine receptors from calf brain and their splenocytes fused with NS1 myeloma cells. Hybrid cultures were grown and selected for production of antibodies on the basis of enzyme immunoassays on calf and rat forebrain membrane preparations. Thirty‐four clones were retained and six of them further subcloned. Two of these subclones produced antibodies that selectively recognized muscarinic acetylcholine receptor‐bearing membranes. The M‐35b antibodies interacted only with native digitonin‐solubilized receptors, and not with denatured receptors. The M‐23c antibodies did not react with active digitonin‐solubilized receptors but recognized the denatured form. The M‐23c antibodies should thus be useful in the purification of the receptor and its precursor translation products, while the M‐35b antibodies could be used for the immunocytochemical localization of the receptor in cells and tissues of different species.