Lande W M, Thiemann P V, Fisher K A, Mentzer W C
Biochim Biophys Acta. 1984 Nov 21;778(1):105-11. doi: 10.1016/0005-2736(84)90453-x.
Cylindrin, a macromolecule isolated from the human erythrocyte, and the band 7 proteins of the erythrocyte membrane were analyzed by one- and two-dimensional electrophoresis. Cylindrin was recovered from both the cytosol and cell membranes of hypotonically lysed erythrocytes, and its identity was confirmed by electrophoresis and transmission electron microscopy. Cylindrin from either source produced eight bands on one-dimensional SDS gels, and seventeen spots on two-dimensional gels, revealing a more complex composition than previously reported. It is unlikely that this complexity was due to proteolysis, since preparations of cylindrin with various protease inhibitors gave the same electrophoretic patterns. Mixing experiments showed that the polypeptide subunits of the cylindrin complex are distinct from the band 7 proteins of the erythrocyte membrane. This finding failed to support a role for the cylindrin macromolecule in the permeability disorders of the erythrocyte membrane associated with a missing band 7 protein.
从人红细胞中分离出的大分子圆柱蛋白以及红细胞膜的带7蛋白，通过一维和二维电泳进行了分析。圆柱蛋白可从低渗裂解红细胞的胞质溶胶和细胞膜中回收，其身份通过电泳和透射电子显微镜得以确认。来自任一来源的圆柱蛋白在一维SDS凝胶上产生八条带，在二维凝胶上产生十七个斑点，显示出比先前报道更为复杂的组成。这种复杂性不太可能是由于蛋白水解造成的，因为添加各种蛋白酶抑制剂的圆柱蛋白制剂给出了相同的电泳图谱。混合实验表明，圆柱蛋白复合物的多肽亚基与红细胞膜的带7蛋白不同。这一发现不支持圆柱蛋白大分子在与缺失带7蛋白相关的红细胞膜通透性障碍中起作用。
