{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,15]],"date-time":"2026-10-15T00:51:04Z","timestamp":1792025464559,"version":"4.4.0"},"reference-count":0,"publisher":"American Physiological Society","issue":"2","content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["American Journal of Physiology-Cell Physiology"],"published-print":{"date-parts":[[1995,8,1]]},"abstract":"<jats:p> External iodide (I-o) inhibits AE1 (band 3)-mediated anion exchange in human red blood cells by binding to a noncompetitive inhibitory site, the external halide modifier site. External N-(4-azido-2-nitrophenyl)-2-aminoethyl sulfonate (NAP-taurine) and N-(4-isothiocyano-2-nitrophenyl)-2-aminoethyl sulfonate (NIP-taurine) also inhibit Cl- exchange noncompetitively. Increasing I-o decreases the inhibitory potency of NIP-taurine in a competitive fashion; this effect is not due to I- binding to the transport site, which has little effect on the NIP-taurine affinity. Bis(sulfosuccinimidyl)-suberate (BSSS) abolishes the noncompetitive inhibitory effect of I-o and greatly reduces the inhibitory effect of NAP-taurine. Together with previous work, these data suggest that external halides, such as I-, Br-, and probably also Cl-, bind to the same noncompetitive inhibitory site as do NAP- and NIP-taurine and that these reagents can be used to label the halide modifier site. Lys-539, a probable reaction site of BSSS, lies within the same segment of AE1 that is labeled by NAP-taurine and thus may be part of the modifier site. <\/jats:p>","DOI":"10.1152\/ajpcell.1995.269.2.c410","type":"journal-article","created":{"date-parts":[[2017,12,24]],"date-time":"2017-12-24T18:29:02Z","timestamp":1514140142000},"page":"C410-C416","source":"Crossref","is-referenced-by-count":7,"title":["NIP- and NAP-taurine bind to external modifier site of AE1 (band 3), at which iodide inhibits anion exchange"],"prefix":"10.1152","volume":"269","author":[{"given":"P. A.","family":"Knauf","sequence":"first","affiliation":[{"name":"Department of Biophysics, University of Rochester School of Medicine,New York 14642, USA."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"L. J.","family":"Spinelli","sequence":"additional","affiliation":[{"name":"Department of Biophysics, University of Rochester School of Medicine,New York 14642, USA."}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"24","container-title":["American Journal of Physiology-Cell Physiology"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/journals.physiology.org\/doi\/pdf\/10.1152\/ajpcell.1995.269.2.C410","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2024,6,17]],"date-time":"2024-06-17T19:39:01Z","timestamp":1718653141000},"score":1,"resource":{"primary":{"URL":"https:\/\/journals.physiology.org\/doi\/10.1152\/ajpcell.1995.269.2.C410"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[1995,8,1]]},"references-count":0,"journal-issue":{"issue":"2","published-print":{"date-parts":[[1995,8,1]]}},"alternative-id":["10.1152\/ajpcell.1995.269.2.C410"],"URL":"https:\/\/doi.org\/10.1152\/ajpcell.1995.269.2.c410","relation":{},"ISSN":["0363-6143","1522-1563"],"issn-type":[{"value":"0363-6143","type":"print"},{"value":"1522-1563","type":"electronic"}],"subject":[],"published":{"date-parts":[[1995,8,1]]}}}