Soldatov N M
Biokhimiia. 1988 Sep;53(9):1418-26.
A microsomal fraction of rabbit skeletal muscle was sed for the isolation of a dihydropyridine (DHP) receptor, a putative potential-dependent calcium channel. The receptor purification was followed by the binding of 3H-labeled riodipine derivative which possesses a high affinity for digitonin-solubilized DHP receptor. The DHP-Sepharose affinity chromatography of an enriched receptor fraction allowed to isolate a receptor, 60-70% homogeneous on the basis of DHP-binding activity. SDS gel electrophoresis showed that the purified receptor is composed of two subunits with molecular masses of 160 and 53 kD. The large subunit changes its electrophoretic mobility after the reduction of disulfide bonds.
用兔骨骼肌微粒体部分来分离二氢吡啶（DHP）受体，这是一种假定的电压依赖性钙通道。受体纯化后，用对洋地黄皂苷增溶的DHP受体具有高亲和力的3H标记的硝苯地平衍生物进行结合。对富集的受体部分进行DHP-琼脂糖亲和层析，可分离出一种基于DHP结合活性而言纯度为60%-70%的受体。SDS凝胶电泳显示，纯化后的受体由两个亚基组成，分子量分别为160 kD和53 kD。还原二硫键后，大亚基的电泳迁移率发生变化。
