Identification by site-directed mutagenesis of Lys-558 as the covalent attachment site of H2DIDS in the mouse erythroid band 3 protein
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Biochemistry,Biophysics
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2. 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)
3. 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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