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PMID: 7035467 Published · ppublish English Journal Article

Immunocytochemical localization of the lens main intrinsic polypeptide (MIP26) in communicating junctions.

The Journal of cell biology ·Vol. 92 ·No. 1 ·1982-01-00 ·Pages 213-20

Bok D, Dockstader J, Horwitz J

Abstract

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.

MeSH Terms
Aquaporins Cell Communication Cell Membrane/analysis Eye Proteins/analysis Immunologic Techniques Intercellular Junctions/analysis Lens, Crystalline/analysis,immunology Membrane Glycoproteins Membrane Proteins/analysis Molecular Weight
Chemicals
Aquaporins Eye Proteins Membrane Glycoproteins Membrane Proteins aquaporin 0
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Bok D
Dockstader J
Horwitz J
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42 references, click to expand
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Article Info
Journal
The Journal of cell biology
Abbr.
J Cell Biol
ISSN
0021-9525
DOI
10.1083/jcb.92.1.213
Published
1982-01-00
Pages
213-20
Language
English
Region
United States
NLM ID
0375356
PMCID
PMC2112001
Subset
IM
External Links
PubMed source DOI: 10.1083/jcb.92.1.213 PMC Full Text View journal details
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