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.
Article| January 01 1982
Immunocytochemical localization of the lens main intrinsic polypeptide (MIP26) in communicating junctions.
Online Issn: 1540-8140
Print Issn: 0021-9525
J Cell Biol (1982) 92 (1): 213–220.
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D Bok, J Dockstader, J Horwitz; Immunocytochemical localization of the lens main intrinsic polypeptide (MIP26) in communicating junctions.. J Cell Biol 1 January 1982; 92 (1): 213–220. doi: https://doi.org/10.1083/jcb.92.1.213
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