Molecular organization of gap junctions.

J. P. Revel, B. J. Nicholson, S. B. Yancey

Research output: Contribution to journalArticlepeer-review

19 Scopus citations

Abstract

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.

Original languageEnglish (US)
Pages (from-to)2672-2677
Number of pages6
JournalFederation Proceedings
Volume43
Issue number12
StatePublished - Sep 1984
Externally publishedYes

ASJC Scopus subject areas

  • Medicine(all)

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