Interaction of SR 33557 with skeletal muscle calcium channel blocker receptors in the baboon: characterization of its binding sites.

摘要: A procedure for the isolation of primate skeletal microsomal membranes was initiated. Membranes exhibited specific enzymatic markers such as 59-nucleotidase, Ca++,Mg(++)-adenosine triphosphatase and an ATP-dependent calcium uptake. Baboon microsomes bound specifically with high-affinity potent Ca++ channel blockers dihydropyridine, phenylalkylamine benzothiazepine derivatives. Scatchard analysis equilibrium binding assays [3H](+)-PN 200-110, [3H](-)-desmethoxyverapamil [( 3H](-)-D888) [3H]-d-cis-dilitiazem were consistent a single class sites three radioligands. The pharmacological profile SR 33557, original compound antagonist properties, investigated using radioligand studies. 33557 totally inhibited main classes effectors interacted allosterically them. In addition, high affinity to homogeneous population in baboon muscle.