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Specific 33-residue repeat(s) of erythrocyte ankyrin associate with the anion exchanger.
Davis LH, Otto E, Bennett V. Davis LH, et al. Among authors: bennett v. J Biol Chem. 1991 Jun 15;266(17):11163-9. J Biol Chem. 1991. PMID: 1828247 Free article.
Erythrocyte ankyrin contains an 89-kDa domain (residues 2-827) comprised almost entirely of 22 tandem repeats of 33 amino acids which are responsible for the high affinity interaction of ankyrin with the anion exchanger (Davis, L., and Bennett, V. (1990) J. Biol. Ch …
Erythrocyte ankyrin contains an 89-kDa domain (residues 2-827) comprised almost entirely of 22 tandem repeats of 33 amino acids which are re …
Mapping the binding sites of human erythrocyte ankyrin for the anion exchanger and spectrin.
Davis LH, Bennett V. Davis LH, et al. Among authors: bennett v. J Biol Chem. 1990 Jun 25;265(18):10589-96. J Biol Chem. 1990. PMID: 2141335 Free article.
The 89-kDa domain is comprised of a series of tandem repeats of 33 amino acids that extend from residues 35 to 778 (Lux, S., John, K., and Bennett, V. (1990) Nature 344, 36-42). The activity of residues 403-779 demonstrates that the 33-amino acid repeats of the 89-k …
The 89-kDa domain is comprised of a series of tandem repeats of 33 amino acids that extend from residues 35 to 778 (Lux, S., John, K., and …
461 results