Soldatov N M
Biokhimiia. 1988 Oct;53(10):1600-11.
Up to 80% of the dihydropyridine receptor is solubilized from transverse tubules of rabbit skeletal muscle by 3-[(3-cholamidopropyl)-dimethylammonium]-2-oxy-1-propane sulfonate (CHAPSO). The DHP receptor is an oligomeric complex made up of two subunits with molecular masses of 160 and 53 kD as shown by DHP-Sepharose affinity chromatography and SDS gel electrophoresis of specifically eluted proteins. The reduction of disulfide bridges of the 160 kD subunit is accompanied by a decrease in its apparent molecular mass up to 125 kD. A method is proposed for preparative isolation of the DHP receptor which is based on ion-exchange chromatography and WGA-Sepharose chromatography. Individual subunits of DHP receptor were isolated by Sepharose 4B gel filtration in SDS; their amino acid composition was determined. Both the 160 and 53 kD subunits are N-glycosylated, and the oligosaccharide portions make up to 7.5% and 6.6%, respectively.
高达80%的二氢吡啶受体可被3-[(3-胆酰胺丙基)-二甲基铵]-2-氧代-1-丙烷磺酸盐（CHAPSO）从兔骨骼肌的横管中溶解出来。如通过二氢吡啶-琼脂糖亲和色谱法以及对特异性洗脱蛋白质进行十二烷基硫酸钠凝胶电泳所示，二氢吡啶受体是一种由分子量分别为160 kD和53 kD的两个亚基组成的寡聚复合物。160 kD亚基的二硫键还原伴随着其表观分子量降至125 kD。本文提出了一种基于离子交换色谱法和麦胚凝集素-琼脂糖色谱法对二氢吡啶受体进行制备性分离的方法。通过在十二烷基硫酸钠中进行琼脂糖4B凝胶过滤分离出二氢吡啶受体的各个亚基；测定了它们的氨基酸组成。160 kD和53 kD的亚基均为N-糖基化，寡糖部分分别占7.5%和6.6%。
