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Isolation and characterisation of arthropod gap junctions
Author(s) -
Finbow Malcolm E.,
Buultjens T.Eldridge J.,
Lane Nancy J.,
Shuttleworth John,
Pitts John D.
Publication year - 1984
Publication title -
the embo journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.484
H-Index - 392
eISSN - 1460-2075
pISSN - 0261-4189
DOI - 10.1002/j.1460-2075.1984.tb02125.x
Subject(s) - nephrops norvegicus , hepatopancreas , biology , trimer , biochemistry , protein subunit , arthropod , peptide , tetramer , antigenicity , crustacean , microbiology and biotechnology , decapoda , enzyme , antibody , dimer , zoology , chemistry , paleontology , organic chemistry , gene , immunology
Gap junctions have been isolated from the hepatopancreas of the crustacean arthropod, Nephrops norvegicus (Norway lobster). SDS‐PAGE of these preparations shows two major protein bands, mol. wt. 18 000 (18 K) and mol. wt. 28 000 (28 K). The 18‐K and 28‐K proteins are interconvertible, cannot be distinguished by two dimensional tryptic and chymotryptic peptide mapping, and therefore appear to be different (most likely monomeric and dimeric) forms of the same protein. The protein can also aggregate to higher multimeric forms mol. wt. 38 000 (presumed trimer), and mol. wt. 52 000 (presumed tetramer). The buoyant density of the isolated gap junctions in continuous potassium iodide gradients is 1.260 g/cm 3 . The junctions are progressively solubilized in increasing SDS concentrations, mostly between 0.1% and 0.2% SDS, and this is accompanied by the release of the 18‐K and 28‐K forms of the junctional protein. The Nephrops hepatopancreas 18‐K junctional protein has antigenic determinants in common with the vertebrate 16‐K junctional protein as shown by cross‐reactivity with two different affinity purified antibody preparations. However, no detectable similarity can be seen between the major 125 I‐labelled tryptic and chymotrytpic peptides of the Nephrops hepatopancreas 18‐K protein and the mouse liver 16‐K protein.

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