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Effects of the transport site conformation on the binding of external NAP-taurine to the human erythrocyte anion exchange system. Evidence for intrinsic asymmetry
External N-(4-azido-2-nitrophenyl)-2-aminoethylsulfonate (NAP-taurine) inhibits human red cell chloride exchange by binding to a site that is distinct from the chloride transport site. Increases in the intracellular chloride concentration (at constant external chloride) cause an increase in the inhi...
| Formato: | Texto |
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| Lenguaje: | English |
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The Rockefeller University Press
1984
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| Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2215659/ https://www.ncbi.nlm.nih.gov/pubmed/6736916 |