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Am J Physiol Cell Physiol 269: C410-C416, 1995;
0363-6143/95 $5.00
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AJP - Cell Physiology, Vol 269, Issue 2 C410-C416, Copyright © 1995 by American Physiological Society

ARTICLES

NIP- and NAP-taurine bind to external modifier site of AE1 (band 3), at which iodide inhibits anion exchange

P. A. Knauf and L. J. Spinelli
Department of Biophysics, University of Rochester School of Medicine, New York 14642, USA.

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.


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[Abstract] [Full Text] [PDF]


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