Inhibition of mouse erythroid band 3-mediated chloride transport by site-directed mutagenesis of histidine residues and its reversal by second site mutation of Lys 558, the locus of covalent H2DIDS binding. [electronic resource]
- Biochemistry Jul 1995
- 9315-24 p. digital
Publication Type: Comparative Study; Journal Article; Research Support, Non-U.S. Gov't
0006-2960
10.1021/bi00029a006 doi
4,4'-Diisothiocyanostilbene-2,2'-Disulfonic Acid--analogs & derivatives Amino Acid Sequence Animals Anion Exchange Protein 1, Erythrocyte--chemistry Biological Transport Cell Membrane--metabolism Chlorides--metabolism Cross-Linking Reagents Electrophoresis, Polyacrylamide Gel Erythrocytes--metabolism Female Histidine Lysine Mice Molecular Sequence Data Mutagenesis, Site-Directed Oocytes--metabolism Point Mutation Protein Biosynthesis Protein Folding Protein Structure, Secondary Recombinant Proteins--chemistry Reticulocytes--metabolism Xenopus laevis