Abstract
The membranous segment of the anion transport protein (band 3) of the human erythrocyte membrane has been shown [T. L. Miller and R. J. Smith, Archs Biochem. Biophys. 250, 128 (1986)] to be destabilized by relatively low concentrations of many hydroxychloroaromatic compounds (HO-Cl x -Ar), including hydroxychlorodiphenyl ethers (HO-Cl x ,-DPE), major contaminants of technical grade pentachlorophenol (PCP). In the present study, HO-Cl x -DPE also caused a concentration-dependent inhibition of the rate of sulfate exchange mediated by band 3 in human erythrocytes. The most active compound studied, 2-HO-Cl 9-DPE, was about nine times more potent in inhibiting sulfate exchange than 2-HO-′,4,4′-Cl 3-DPE, the least active compound studied. The potency of HO-Cl x ,-DPE as inhibitors of anion exchange generally increased with the degree of chlorination. The concentration-dependent decreases in the sulfate exchange rate elicited by 2-HO-Cl 9-DPE and 2-HO-2′,4,4′-Cl 3-DPE paralleled the effects of these compounds on the stability of band 3.
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