Inhibition of anion transport in human red blood cells by 5,5′-dithiobis(2-nitrobenzoic acid)
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Biochemistry,Biophysics
Reference21 articles.
1. Erythrocyte Anion Exchange and the Band 3 Protein: Transport Kinetics and Molecular Structure
2. Membrane proteins related to anion permeability of human red blood cells
3. 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)
4. Synthesis of tritiated 4,4′-diisothiocyano-2,2′-stilbene disulfonic acid ([3H]DIDS) and its covalent reaction with sites related to anion transport in human red blood cells
5. Anion transport across the erythrocyte membrane, in situ proteolysis of band 3 protein, and cross-linking of proteolytic fragments by 4,4′-diisothiocyano dihydrostilbene-2,2′-disulfonate
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