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KMID : 0380219940270040335
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Journal of Biochemistry and Molecular Biology
1994 Volume.27 No. 4 p.335 ~ p.341
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Purification and Characterization of a Major Gap Juction Channel-Forming Protein in Rat Liver
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Abstract
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Abstract:
@EN Connexin 32, the major protein that forms gap junction channels in rat liver tissue, was solubilized and purified by immunoaffinity chromatography. A monoclonal antibody recognizing a cytoplasmic domain of connexin 32 was immobilized onto
CNBr-activated Sepharose beads. The immunobeads were used for one-step purification of connexin 32 from the triton lX-100 solubilize plasma membrane fraction of rat liver tissue. The connexin 32 obtained by this immunoaffinity method was highly
pure. In
contrast to the conventional methods that isolate an intact gap junction membrane, this rapid procedure does not expose the protein to denaturing conditions, and yields connexin 32 which can be readily incorporated into liposomes for use in
reconstitution studes. Structural studies with gel-filtration chromatography and negative-staining electron microscopy showed that the immunoaffinity-purified connexin 32 is present as hexameric forms.
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