title: Activity of the anion exchange protein (band 3) of human erythrocytes as affected by hydroxychloroaromatic chemicals.
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 chi-Ar), including hydroxychlorodiphenyl ethers (HO-Cl chi-DPE), major contaminants of technical grade pentachlorophenol (PCP). In the present study, HO-Cl chi-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-Cl9-DPE, was about nine times more potent in inhibiting sulfate exchange than 2-HO-2',4,4'-Cl3-DPE, the least active compound studied. The potency of HO-Cl chi-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-Cl9-DPE and 2-HO-2',4,4'-Cl3-DPE paralleled the effects of these compounds on the stability of band 3.
authors: Department of Agricultural Chemistry, Oregon State University, Corvallis 97331.
authors: R J
authors: RJ
authors: Smith
authors: T L
authors: TL
authors: Miller
mesh_terms: D001457:Anion Exchange Protein 1, Erythrocyte / Q000037:antagonists & inhibitors*; D001692:Biological Transport / Q000187:drug effects; D002733:Chlorophenols / Q000378:metabolism / Q000494:pharmacology*; D004910:Erythrocyte Membrane / Q000187:drug effects* / Q000378:metabolism; D006358:Hot Temperature; D006801:Humans; D066298:In Vitro Techniques; D008012:Lidocaine / Q000378:metabolism / Q000494:pharmacology; D013329:Structure-Activity Relationship; D013431:Sulfates / Q000097:blood
chemical_list: D001457:Anion Exchange Protein 1, Erythrocyte; D002733:Chlorophenols; D013431:Sulfates; D008012:Lidocaine