Characterization of the Band 3 substrate site in human red cell ghosts by NDS-TEMPO, a disulfonatostilbene spin probe: The function of protons in NDS-TEMPO and substrate-anion binding in relation to anion transport-Reference-Cited by-同舟云学术

Characterization of the Band 3 substrate site in human red cell ghosts by NDS-TEMPO, a disulfonatostilbene spin probe: The function of protons in NDS-TEMPO and substrate-anion binding in relation to anion transport

Published:1986-06 Issue:2 Volume:91 Page:129-146
ISSN:0022-2631
Container-title:The Journal of Membrane Biology
language:en
Short-container-title:J. Membrain Biol.

Author:

Kaufmann E.,Eberl G.,Schnell K. F.

Publisher

Springer Science and Business Media LLC

Subject

Cell Biology,Physiology,Biophysics

Link

http://link.springer.com/content/pdf/10.1007/BF01925790.pdf

Reference56 articles.

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2. Bodemann, H., Passow, H. 1972. Factors controlling the resealing of the membrane of human erythrocyte ghosts after hypotonic hemolysis.J. Membrane Biol. 8:1–26

3. Brahm, J. 1977. Temperature-dependence of chloride transport kinetics in human red blood cells.J. Gen. Physiol. 70:283–306

4. Cabantchik, Z.I., Rothstein, A. 1972. The nature of the membrane sites controlling anion permeability of human red blood cells as determined by studies with disulfonic stilbene derivatives.J. Membrane Biol. 10:311–330

5. Cabantchik, Z.I., Rothstein, A. 1974. Membrane proteins related to anion permeability of human red blood cells. I. Localization of disulfonic stilbene binding sites in proteins involved in permeation.J. Membrane Biol. 15:207–226

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