Schmid A, Barhanin J, Coppola T, Borsotto M, Lazdunski M
Biochemistry. 1986 Jun 17;25(12):3492-5. doi: 10.1021/bi00360a002.
Previous purification studies of the 1,4-dihydropyridine receptor associated with the calcium channel of rabbit skeletal muscle had shown that it is composed of a large glycoprotein of Mr 140,000-145,000 associated with a smaller component of Mr 32,000-34,000. Specific antisera have now been prepared against the larger component (anti-140 serum) and the smaller one (anti-32 serum). The specificity of these two antisera has been analyzed by immunoblot assays with microsomal preparations of rabbit skeletal muscle. Under disulfide-reducing conditions the anti-140 serum specifically labeled a polypeptide of Mr 140,000 while the anti-32 serum labeled three polypeptides of Mr 32,000, 29,000, and 26,000. Under nonreducing conditions both the anti-140 and the anti-32 sera specifically recognized a single large polypeptide of Mr 170,000. The same type of approach showed that the dihydropyridine receptor in cardiac and smooth muscles had a polypeptide composition similar to that found in skeletal muscle with a large polypeptide of Mr 170,000-176,000 made of two different chains of about Mr 140,000 and 34,000-32,000 associated by disulfide bridges.
先前对与兔骨骼肌钙通道相关的1,4 - 二氢吡啶受体的纯化研究表明，它由一个分子量为140,000 - 145,000的大糖蛋白和一个分子量为32,000 - 34,000的较小成分组成。现已制备出针对较大成分（抗140血清）和较小成分（抗32血清）的特异性抗血清。通过兔骨骼肌微粒体制剂的免疫印迹分析来检测这两种抗血清的特异性。在二硫键还原条件下，抗140血清特异性标记了一条分子量为140,000的多肽，而抗32血清标记了分子量为32,000、29,000和26,000的三条多肽。在非还原条件下，抗140血清和抗32血清都特异性识别一条分子量为170,000的大多肽。同样的方法表明，心脏和平滑肌中的二氢吡啶受体具有与骨骼肌中相似的多肽组成，即一条分子量为170,000 - 176,000的大多肽，由两条不同的链组成，一条约为分子量140,000，另一条为34,000 - 32,000，通过二硫键相连。
