Separation of dihydropyridine binding sites from cardiac junctional sarcoplasmic reticulum.
When microsomes from feline ventricular muscle are centrifuged on continuous linear sucrose gradients, the major peak for the distribution pattern of the dihydropyridine binding sites corresponds in position and shape with the distribution of the Mr 300K polypeptide marker for junctional sarcoplasmic reticulum (SR). Plasma membrane vesicles are also present in those gradient fractions and appear to be joined to the junctional SR as native dyads. We now report that when such putative dyads are passed through the French press, both the dihydropyridine binding sites and the plasma membrane marker band together at a new isopycnic point distinct from the junctional SR. We conclude that as has been found in the skeletal muscle system the dihydropyridine binding sites are a marker for the junctional domain of the plasma membrane and that separation of the dyad components of the mammalian myocardium can be attained.
D000818:Animals; D001665:Binding Sites; D015220:Calcium Channels; D002415:Cats; D004095:Dihydropyridines; D066298:In Vitro Techniques; D008861:Microsomes / Q000378:metabolism; D009206:Myocardium / Q000378:metabolism*; D011725:Pyridines / Q000378:metabolism*; D011976:Receptors, Muscarinic / Q000378:metabolism; D011978:Receptors, Nicotinic / Q000378:metabolism*; D012519:Sarcoplasmic Reticulum / Q000378:metabolism*
D015220:Calcium Channels; D004095:Dihydropyridines; D011725:Pyridines; D011976:Receptors, Muscarinic; D011978:Receptors, Nicotinic; C038806:1,4-dihydropyridine