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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...

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Библиографические подробности
Формат: Artigo
Язык:Inglês
Опубликовано: The Rockefeller University Press 1984
Предметы:
Online-ссылка:https://ncbi.nlm.nih.gov/pmc/articles/PMC2215659/
https://ncbi.nlm.nih.gov/pubmed/6736916
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