A study of the relationship between inhibition of anion exchange and binding to the red blood cell membrane of 4,4′-diisothiocyano stilbene-2,2′-disulfonic acid (DIDS) and its dihydro derivative (H2DIDS)-Reference-Cited by-同舟云学术

A study of the relationship between inhibition of anion exchange and binding to the red blood cell membrane of 4,4′-diisothiocyano stilbene-2,2′-disulfonic acid (DIDS) and its dihydro derivative (H2DIDS)

Published:1976-12 Issue:1 Volume:29 Page:147-177
ISSN:0022-2631
Container-title:The Journal of Membrane Biology
language:en
Short-container-title:J. Membrain Biol.

Author:

Lepke S.,Fasold H.,Pring M.,Passow H.

Publisher

Springer Science and Business Media LLC

Subject

Cell Biology,Physiology,Biophysics

Link

http://link.springer.com/content/pdf/10.1007/BF01868957.pdf

Reference26 articles.

1. Acton, F.S. 1959. Analysis of Straight Line Data. Dover Publications, Inc., New York

2. 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

3. Cabantchik, Z.I., Rothstein, A. 1974. Membrane proteins related to anion permeability of human red blood cells. II. Effects of proteolytic enzymes on disulfonic stilbene sites of surface proteins.J. Membrane Biol. 15:227

4. 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

5. Dalmark, M. 1975. Chloride transport in human red cells.J. Physiol. (London) 250:39

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