Simultaneous light and electron microscopic observation of immunolabeled liver 27 KD gap junction protein on ultra-thin cryosections. | Zendy

Rolf Dermietzel | Zendy; Brett D. Yancey | Zendy; U Janssen-Timmen | Zendy; Otto Traub | Zendy; Klaus Willecke | Zendy; J P Revel | Zendy

Open Access

Simultaneous light and electron microscopic observation of immunolabeled liver 27 KD gap junction protein on ultra-thin cryosections.

Author(s) -

Rolf Dermietzel,

Brett D. Yancey,

U Janssen-Timmen,

Otto Traub,

Klaus Willecke,

J P Revel

Publication year - 1987

Publication title -

journal of histochemistry and cytochemistry

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 0.971

H-Index - 124

eISSN - 1551-5044

pISSN - 0022-1554

DOI - 10.1177/35.3.3029214

Subject(s) - immunolabeling , immunogold labelling , gap junction , polyclonal antibodies , thin section , biophysics , electron microscope , monoclonal antibody , immunofluorescence , chemistry , ultrastructure , biology , materials science , antibody , microbiology and biotechnology , immunohistochemistry , anatomy , optics , physics , mineralogy , immunology , intracellular

We report on immunolabeling of gap junction protein in rat liver. Simultaneous light and electron microscopic immunolabeling of ultra-thin frozen sections was performed to confirm that the antigenic targets of polyclonal antibodies and a monoclonal 27 KD antibody (12/1 C5) are the gap junctions. Our results clearly demonstrate that the immunoreactive sites determined by indirect immunofluorescence correspond to immunogold-labeled gap junctions identified in the same section according to electron microscopic criteria. Our results also support the concept that the 27 KD protein is a major constituent of gap junctions.

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