THE STUDY OF THE ANION TRANSPORT PROTEIN (‘BAND 3 PROTEIN’) IN THE RED CELL MEMBRANE BY MEANS OF TRITIATED 4,4′-DIISOTHIOCYANO-DIHYDROSTILBENE-2,2-DISULFONIC ACID (3H2DIDS)
- 1 January 1982
- book chapter
- Published by Elsevier
Abstract
No abstract availableThis publication has 32 references indexed in Scilit:
- Interaction of tritium-labeled H2DIDS (4,4′-diisothiocyano-1,2,diphenyl ethane-2,2′disulfonic acid) with the ehrlich mouse ascites tumor cellThe Journal of Membrane Biology, 1979
- Proteolytic degradation of human erythrocyte band 3 by membrane-associated protease activityThe Journal of Membrane Biology, 1979
- 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 cellsThe Journal of Membrane Biology, 1977
- Membrane proteins related to anion permeability of human red blood cellsThe Journal of Membrane Biology, 1974
- Membrane proteins related to anion permeability of human red blood cellsThe Journal of Membrane Biology, 1974
- The effects of maleic anhydride on the ionic permeability of red cellsThe Journal of Membrane Biology, 1972
- Effects of pronase on passive ion permeability of the human red blood cellThe Journal of Membrane Biology, 1971
- Action of 1-fluoro-2,4-dinitrobenzene on passive ion permeability of the human red blood cellThe Journal of Membrane Biology, 1971
- The permeability of the human red blood cell to sulfate ionsThe Journal of Membrane Biology, 1971
- Chemical modifiers of passive ion permeability of the erythrocyte membraneCellular and Molecular Life Sciences, 1969