Bok D, Dockstader J, Horwitz J
J Cell Biol. 1982 Jan;92(1):213-20. doi: 10.1083/jcb.92.1.213.
Plasma membranes of vertebrate lens fiber cells contain a major intrinsic polypeptide with an apparent molecular weight of 26,000 (MIP26). These plasma membranes are extremely rich in communicating junctions, and it has been suggested that MIP26 is a component of them. MIP26 was purified from cow lenses using preparative SDS gel electrophoresis followed by hydroxylapatite column chromatography. From gel electrophoresis patterns and aggregational properties it was concluded that the MIP26 preparation was homogeneous. The purified MIP26 was used to produce monospecific antibodies in rabbits as assessed by double immunodiffusion and crossed immunoelectrophoresis of purified MIP26 and solubilized lens plasma membranes against the antiserum. Indirect immunocytochemical studies were performed on open and closed lens plasma membrane vesicles by incubation in anti-MIP antiserum followed by ferritin-conjugated goat antirabbit IgG. The conjugate bound unequivocally to lens communicating junctions, indicating that MIP26 is a component of these structures.
脊椎动物晶状体纤维细胞的质膜含有一种主要内在多肽，其表观分子量为26,000（MIP26）。这些质膜富含通讯连接，有人认为MIP26是其组成成分之一。采用制备性SDS凝胶电泳，随后进行羟基磷灰石柱层析，从牛晶状体中纯化出MIP26。根据凝胶电泳图谱和聚集特性得出结论，MIP26制剂是纯一的。通过对纯化的MIP26和溶解的晶状体质膜与抗血清进行双向免疫扩散和交叉免疫电泳评估，使用纯化的MIP26在兔体内产生单特异性抗体。通过在抗MIP抗血清中孵育，然后用铁蛋白偶联的山羊抗兔IgG对开放和封闭的晶状体质膜小泡进行间接免疫细胞化学研究。该偶联物明确地与晶状体通讯连接结合，表明MIP26是这些结构的一个组成成分。
