Kouvonen I
Biochim Biophys Acta. 1981 Aug 20;646(2):268-73. doi: 10.1016/0005-2736(81)90333-3.
The pig intestinal intrinsic factors receptor has been isolated and dissociated into its alpha and beta subunits. The beta subunit was found to be more hydrophobic than the alpha subunit. In a detergent solution only the alpha subunit was accessible to digestion with papain. The whole isolated receptor was introduced into artificial single bilayer liposomes where is apparently was randomly oriented. Liposomes containing the receptor were digested with papain and the polypeptide segments that stayed in the lipid fraction were extracted and analyzed using sodium dodecyl sulfate polyacrylamide gel electrophoresis. Four species were found with Mr values of 23 000, 45 000, 70 000 and 86 000.
猪肠内因子受体已被分离并解离成其α和β亚基。发现β亚基比α亚基更具疏水性。在去污剂溶液中，只有α亚基可被木瓜蛋白酶消化。将整个分离的受体引入人工单层脂质体中，在那里它显然是随机取向的。用木瓜蛋白酶消化含有受体的脂质体，提取留在脂质部分的多肽片段，并使用十二烷基硫酸钠聚丙烯酰胺凝胶电泳进行分析。发现了四种分子量分别为23000、45000、70000和86000的物种。
