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Mutational analysis of phenylalanine beta 85 in the valine beta 6 acceptor pocket during hemoglobin S polymerization.
Adachi K, Reddy LR, Reddy KS, Surrey S. Adachi K, et al. Protein Sci. 1995 Jul;4(7):1272-8. doi: 10.1002/pro.5560040703. Protein Sci. 1995. PMID: 7670370 Free PMC article.
This is in contrast to deoxy Hb S containing Phe-beta 88, Ala-beta 88, Glu-beta 88, or Glu-beta 85, which polymerized with no clear delay time (Adachi K, Konitzer P, Paulraj CG, Surrey S, 1994, J Biol Chem 269:17477-17480; Adachi K, Reddy LR, Surrey S, …
This is in contrast to deoxy Hb S containing Phe-beta 88, Ala-beta 88, Glu-beta 88, or Glu-beta 85, which polymerized with no clear delay ti …
Role of hydrophobicity of phenylalanine beta 85 and leucine beta 88 in the acceptor pocket for valine beta 6 during hemoglobin S polymerization.
Adachi K, Reddy LR, Surrey S. Adachi K, et al. J Biol Chem. 1994 Dec 16;269(50):31563-6. J Biol Chem. 1994. PMID: 7989324 Free article.
Critical concentrations for polymerization of Hb SF beta 85E and Hb SL beta 88E were 2.4- and 7-fold higher, respectively, than that of Hb S, while the value for Hb SL beta 88E was intermediate between those previously reported for Hb SL beta 88A and Hb SL beta 88F (Adachi …
Critical concentrations for polymerization of Hb SF beta 85E and Hb SL beta 88E were 2.4- and 7-fold higher, respectively, than that of Hb S …
Role of Leu-beta 88 in the hydrophobic acceptor pocket for Val-beta 6 during hemoglobin S polymerization.
Adachi K, Konitzer P, Paulraj CG, Surrey S. Adachi K, et al. J Biol Chem. 1994 Jul 1;269(26):17477-80. J Biol Chem. 1994. PMID: 8021253 Free article.
Deoxy-Hb S containing Phe-beta 88 polymerized without a delay time like Trp-beta 6- and Phe-beta 6-substituted hemoglobins (Adachi, K., Konitzer, P., Kim, J., Welch, N., and Surrey, S. (1993) J. Biol. Chem. 268, 21650-21656). ...
Deoxy-Hb S containing Phe-beta 88 polymerized without a delay time like Trp-beta 6- and Phe-beta 6-substituted hemoglobins (Adachi, …
2,296 results