ACELL October 46/4

نویسندگان

  • SONYA BAHAR
  • CHRISTOPHER T. GUNTER
  • CHERYL WU
  • SCOTT D. KENNEDY
  • PHILIP A. KNAUF
  • Christopher T. Gunter
  • Cheryl Wu
  • Scott D. Kennedy
چکیده

Bahar, Sonya, Christopher T. Gunter, Cheryl Wu, Scott D. Kennedy, and Philip A. Knauf. Persistence of external chloride and DIDS binding after chemical modification of Glu-681 in human band 3. Am. J. Physiol. 277 (Cell Physiol. 46): C791–C799, 1999.—Although its primary function is monovalent anion exchange, the band 3 protein also cotransports divalent anions together with protons at low pH. The putative proton binding site, Glu-681 in human erythrocyte band 3, is conserved throughout the anion exchanger family (AE family). To determine whether or not the monovalent anion binding site is located near Glu-681, we modified this residue with Woodward’s reagent K (N-ethyl-5-phenylisoxazolium-38-sulfonate; WRK). Measurements of Cl2 binding by 35Cl-NMR show that external Cl2 binds to band 3 even when Cl2 transport is inhibited ,95% by WRK modification of Glu-681. This indicates that the external Cl2 binding site is not located near Glu-681 and thus presumably is distant from the proton binding site. DIDS inhibits Cl2 binding even when WRK is bound to Glu-681, indicating that the DIDS binding site is also distant from Glu-681. Our data suggest that the DIDS site and probably also the externally facing Cl2 transport site are located nearer to the external surface of the membrane than Glu-681.

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تاریخ انتشار 1999