Glossmann H, Striessnig J, Hymel L, Schindler H
Institut für Biochemische Pharmakologie, Universität Innsbruck, Austria.
Biomed Biochim Acta. 1987;46(8-9):S351-6.
The L-type calcium channel was purified from guinea-pig skeletal muscle T-tubule membranes. The purified preparation retained the binding activity for 1,4 dihydropyridines, phenylalkylamines and d-cis diltiazem. Four polypeptides with apparent molecular masses of 180-190, 150-155, 55-60 and 28-35 kDa (termed alpha 1, alpha 2, beta and gamma subunit) copurified with reversible drug binding. In photoaffinity labeling experiments only the alpha 1 subunit was shown to carry the drug receptors. Phosphorylation and functional reconstitution experiments revealed that the cAMP dependent phosphorylation of the alpha 1 subunit is responsible for calcium channel regulation.
L型钙通道是从豚鼠骨骼肌T小管膜中纯化出来的。纯化后的制剂保留了对1,4 -二氢吡啶、苯烷基胺和d-顺式地尔硫䓬的结合活性。四种表观分子量分别为180 - 190 kDa、150 - 155 kDa、55 - 60 kDa和28 - 35 kDa的多肽（分别称为α1、α2、β和γ亚基）与可逆药物结合一起共纯化。在光亲和标记实验中，只有α1亚基显示携带药物受体。磷酸化和功能重建实验表明，α1亚基的cAMP依赖性磷酸化负责钙通道的调节。
