Inhibition of anion permeability of sarcoplasmic reticulum vesicles by stilbene derivatives and the identification of an inhibitor-binding protein.
The permeability of sarcoplasmic reticulum vesicles to sulfate ions was inhibited by diisothiocyano-1,2-diphenylethane-2,2'-disulfonic acid (H2DIDS), which is a potent inhibitor of anion permeability in red blood cell membrane. The amount of H2DIDS bound to the vesicles was determined by using [3H]-H2DIDS. Apparent half inhibition of sulfate permeation was observed on the binding of 2.5 mumol/g protein. SDS-polyacrylamide gel electrophoresis on the vesicles treated with [3H]H2DIDS showed that about 10% of the total bound H2DIDS corresponds to a 100 000-dalton protein, but the remaining 90% to non-protein components. The content of the H2DIDS-binding protein was about 0.5 mumol/g protein. These results suggest that the H2DIDS-binding protein is different from the calcium pump protein and is possibly an anion transport system similar to band 3 in red blood cell membrane.
D017878:4,4'-Diisothiocyanostilbene-2,2'-Disulfonic Acid / Q000031:analogs & derivatives*; D012856:4-Acetamido-4'-isothiocyanatostilbene-2,2'-disulfonic Acid / Q000031:analogs & derivatives / Q000494:pharmacology*; D000818:Animals; D000838:Anions; D002352:Carrier Proteins / Q000378:metabolism*; D007700:Kinetics; D008861:Microsomes / Q000378:metabolism; D009132:Muscles / Q000378:metabolism; D010539:Permeability; D011817:Rabbits; D012519:Sarcoplasmic Reticulum / Q000187:drug effects / Q000378:metabolism*; D013267:Stilbenes / Q000494:pharmacology*; D013431:Sulfates / Q000378:metabolism*
D000838:Anions; D002352:Carrier Proteins; D013267:Stilbenes; D013431:Sulfates; D012856:4-Acetamido-4'-isothiocyanatostilbene-2,2'-disulfonic Acid; C018564:dihydro-DIDS; D017878:4,4'-Diisothiocyanostilbene-2,2'-Disulfonic Acid