title: Reconstitution of the purified receptor for calcium channel blockers.
abstract: The purified receptor for calcium channel blockers from rabbit skeletal muscle was reconstituted into phospholipid vesicles. The reconstitution did not alter the stoichiometry of the peptide chains. [3H]PN 200-110 bound to one site with apparent KD and Bmax values of 9.8 nM and 980 pmol/mg protein, respectively. The binding was stereospecific. D-cis-diltiazem and (-) desmethoxyverapamil affected allosterically the binding of dihydropyridines. This demonstrates the coinsertion of specific binding sites for the three calcium channel blocker into phospholipid vesicles.
authors.affiliation: Institut für Physiologische Chemie, Universität des Saarlandes, Homburg/Saar.
authors.forename: M
authors.initials: M
authors.lastname: Sieber
authors.forename: W
authors.initials: W
authors.lastname: Nastainczyk
authors.forename: A
authors.initials: A
authors.lastname: Röhrkasten
authors.forename: F
authors.initials: F
authors.lastname: Hofmann
mesh_terms: D000494:Allosteric Regulation; D000818:Animals; D001665:Binding Sites; D002121:Calcium Channel Blockers / Q000378:metabolism*; D015220:Calcium Channels; D066298:In Vitro Techniques; D007700:Kinetics; D008081:Liposomes; D008970:Molecular Weight; D010455:Peptides / Q000302:isolation & purification; D011817:Rabbits; D011978:Receptors, Nicotinic / Q000302:isolation & purification* / Q000378:metabolism
chemical_list: D002121:Calcium Channel Blockers; D015220:Calcium Channels; D008081:Liposomes; D010455:Peptides; D011978:Receptors, Nicotinic