Identification of a 70,000-D protein in lens membrane junctional domains.
Open Access
- 30 June 1985
- journal article
- research article
- Published by Rockefeller University Press in The Journal of cell biology
- Vol. 101 (1) , 28-35
- https://doi.org/10.1083/jcb.101.1.28
Abstract
A 70,000-D membrane protein (MP70), which is restricted to the eye lens fibers and is present in immunologically homologous form in many vertebrate species, has been identified. By use of anti-MP70 monoclonal antibodies for immunofluorescence microscopy and electron microscopy, this polypeptide was localized in lens membrane junctional domains. Both immunofluorescence microscopy and SDS PAGE reveal an abundance of MP70 in the lens outer cortex that coincides with a high frequency of fiber gap junctions in the same region.This publication has 55 references indexed in Scilit:
- Biochemical and structural features of chick lens gap junctionsExperimental Eye Research, 1981
- A simple method of reducing the fading of immunofluorescence during microscopyJournal of Immunological Methods, 1981
- The surface morphology of embryonic and adult chick lens‐fiber cellsJournal of Anatomy, 1980
- Gap junction dynamics: reversible effects of hydrogen ions.The Journal of cell biology, 1980
- Lens metabolic cooperation: a study of mouse lens transport and permeability visualized with freeze-substitution autoradiography and electron microscopy.The Journal of cell biology, 1980
- The connexon order in isolated lens gap junctionsJournal of Ultrastructure Research, 1980
- Lens gap junctions and orthogonal arrays are unrelatedFEBS Letters, 1980
- High frequencies of antigen-specific hybridomas: dependence on immunization parameters and prediction by spleen cell analysisJournal of Immunological Methods, 1980
- MEMBRANE-ALTERATIONS DURING CATARACT DEVELOPMENT IN THE NAKANO MOUSE LENS1980
- Lens membranes VII. MIP is an immunologically specific component of lens fiber membranes and is identical with 26K band proteinExperimental Eye Research, 1979