Antibodies to a Covalent Antagonist used to Isolate the Muscarinic Cholinergic Receptor from Rat Brain View Full Text


Ontology type: schema:Chapter     


Chapter Info

DATE

1984

AUTHORS

H. K. Dadi , R. J. Morris , E. C. Hulme , N. J. M. Birdsall

ABSTRACT

To isolate cell-surface receptors a 103–106 fold purification is usually required, which necessitates the use of a powerful affinity step. For this purpose ligand affinity chromatography has proved invaluable provided that the ligand-receptor interaction is not destroyed by solubilization of the receptor or by immobilization of the ligand. The muscarinic cholinergic receptor (MCR) of brain requires over 10,000-fold purification to attain homogeneity [1] and to date a successful ligand chromatography procedure has not been devised. We have therefore pursued an alternative strategy, namely to raise antibodies to the covalent antagonist, propylbenzilylcholinemustard (PrBCM) [2], and to use these to isolate solubilized ligand-receptor complexes (PrBCM-MCR). This approach has been successful with large polypeptide ligands (e.g. insulin [3], transferrin [4], snake α-toxins for the nicotinic cholinergic receptor [5]). Its application to small ligands might be expected to encounter problems since it requires both the antibody and the receptor to bind the ligand simultaneously. However, if a covalent ligand is used the ligand-receptor complex can be denatured, exposing the ligand to the antibody without disrupting its association with the receptor. More... »

PAGES

425-427

Book

TITLE

Investigation of Membrane-Located Receptors

ISBN

978-1-4684-4633-3
978-1-4684-4631-9

Author Affiliations

Identifiers

URI

http://scigraph.springernature.com/pub.10.1007/978-1-4684-4631-9_47

DOI

http://dx.doi.org/10.1007/978-1-4684-4631-9_47

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1031540401


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