Molecular organization of gap junctions.
Highly purified gap junction fractions from heart and liver contain a single major protein component. The proteins isolated from different organs have apparent molecular weights of 26,000-30,000. Peptide mapping and partial sequencing show close homology of the hepatic junctional protein of different species. In contrast, no homologies can be detected when polypeptides from different tissues of the rat were compared by peptide mapping. Preliminary results from partial sequencing, however, show that the amino terminal regions of the liver and heart proteins are related to one another. Sequencing has not yet revealed any such homologies between the lens and the other junction proteins.
D000818:Animals; D007365:Intercellular Junctions / Q000032:analysis / Q000648:ultrastructure*; D008099:Liver / Q000032:analysis / Q000648:ultrastructure; D008563:Membrane Lipids / Q000032:analysis*; D008565:Membrane Proteins / Q000032:analysis*; D008970:Molecular Weight; D009206:Myocardium / Q000032:analysis / Q000648:ultrastructure
D008563:Membrane Lipids; D008565:Membrane Proteins