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Original Article

Anion Transport in Red Blood Cells. III. Sites and Sidedness of Inhibition by High-Affinity Reversible Binding Probes

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Pages 297-322 | Published online: 09 Jul 2009
 

Abstract

Studies of binding of the reversible inhibitor DNDS (for abbreviations, see Nomenclature) and red blood cell membranes revealed 8.6 ± 0.7 × 105 high-affinity binding sites per cell (KD = 0.8 ± 0.4 μM). Under conditions of “mutual depletion,” inhibition studies of anion exchange revealed 8.0 ± 0.7 × 105 DNDS inhibitory sites per cell (KD = 0.87 ± 0.04 μM). Binding and kinetic studies with DNDS indicate that there are 0.8 - 0.9 × 106 functional anion transport sites per red blood cell.

The transport of DNDS displayed high temperature and concentration dependencies, chemical specificity, susceptibility to inhibition by DIDS, and differences between egress and ingress properties.

Under conditions of no DNDS penetration (e.g., 0°C), inhibition of anion exchange by DNDS showed marked sidedness from the outside inhibitions and were demonstrable at micromolar concentrations, whereas from the inside no inhibition occurred even at millimolar concentrations.

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