| Literature DB >> 1130322 |
Abstract
The molecular structure of mouse hepatocyte gap junctions is investigated with corrlated electron microscopy, biochemistry, and x-ray diffraction technics. These studies reveal that the gap junction is composed of a hexagonal lattice of protein subunits, connexons, which pierce the hydrophobic membrane and establish a structural basis for intercellular hydrophilic channels or pores. By digesting liver-cell membranes with trypsin, a preparation of open- and closed-gap junction vesicles can be generated; this preparation will permit direct permeability measurements across the gap junction membranes in an in-vitro system.Entities:
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Year: 1975 PMID: 1130322 DOI: 10.1093/ajcp/63.5.636
Source DB: PubMed Journal: Am J Clin Pathol ISSN: 0002-9173 Impact factor: 2.493