Identification of an anion channel protein from electric organ of Narke japonica |
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Authors: | T Taguchi M Kasai |
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Institution: | Department of Biophysical Engineering Faculty of Engineering Science, Osaka University Toyonaka, Osaka 560 Japan |
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Abstract: | The anion permeability of membrane vesicles prepared from the electric organ of was inhibited by the addition of 4,4′-diisothiocyano-stilbene-2,2′-disulfonic acid (DIDS). The permeability was measured by measuring changes in the scattered-light intensity caused by the osmotic volume change of vesicles; and also by the efflux measurement of ions from the vesicles using radioisotopes. Sodium dodecyl sulfate polyacrylamide gel electrophoresis of membrane vesicles treated with dihydro analog of DIDS (3H]H2DIDS) showed that the H2DIDS binding protein has a molecular weight of 180,000, and exists in membrane vesicles as a dimer formed by a disulfide bond between monomers of molecular weight 90,000. |
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Keywords: | DIDS 4 4′-diisothiocyano-stilbene-2 2′-disulfonic acid 4 4′-diisothiocyano-1 2-diphenyl-ethane-2 2′-disulfonic acid SDS sodium dodecyl sulfate PAS periodic acid-Schiff |
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