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]
Producer: 19950907Description: 9315-24 p. digitalISSN:- 0006-2960
- 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
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Publication Type: Comparative Study; Journal Article; Research Support, Non-U.S. Gov't
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