Reconstitution of the purified receptor for calcium channel blockers.
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.
Sieber
M
M
Institut für Physiologische Chemie, Universität des Saarlandes, Homburg/Saar.
Nastainczyk
W
W
Röhrkasten
A
A
Hofmann
F
F
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
D002121:Calcium Channel Blockers; D015220:Calcium Channels; D008081:Liposomes; D010455:Peptides; D011978:Receptors, Nicotinic