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Journal of Experimental Biology, Vol 203, Issue 9 1497-1502, Copyright © 2000 by Company of Biologists

JOURNAL ARTICLES

The oxalate/sulfate antiporter in lobster hepatopancreas: internal and external binding constants

GA Gerencser, C Burgin, F Robbins and GA Ahearn
Department of Physiology, College of Medicine, University of Florida, Gainesville, FL 32610, USA. gag@phys.med.ufl.edu

Utilizing a purified basolateral plasma membrane vesicle (BLMV) preparation containing a sulfate/oxalate antiporter, it was demonstrated that sulfate exhibited similar binding characteristics to the transporter whether bound internally or externally. It was also demonstrated that oxalate had similar binding characteristics to the antiporter whether it was bound internally or externally. Oxalate had a greater affinity to the transporter than did sulfate. Several organic anions affected binding and, therefore, overall transport by the antiporter. Most notably, sulfate was the only anion that stimulated oxalate uptake into BLMVs, which suggests a conservative binding specificity for the antiporter. 4-Acetamido-4'-isothiocyanostilbene-2,2'-disulfonic acid (SITS) and/or 4,4'-diisothiocyanostilbene-2,2'-disulfonic acid (DIDS) inhibited the transport rate, confirming the existence of oxalate/sulfate exchange by the transporter. These results suggest that oxalate, not sulfate, regulates the transport rate because of its greater affinity to the transporter.


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G. A. Gerencser, F. Robbins, J. Zhang, and G. A. Ahearn
Electrogenic proton-regulated oxalate/chloride exchange by lobster hepatopancreatic brush-border membrane vesicles
J. Exp. Biol., February 1, 2004; 207(4): 571 - 578.
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