Mutational analysis of phenylalanine β85
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Kazuhiko Adachim; Lattupally R. Reddy; Saul Surrey; Konda S. Reddy
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Article
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1995
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Cold Spring Harbor Laboratory Press
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English
⚖ 608 KB
## Abstract Hemoglobin (Hb) S containing Leu, Ala, Thr, or Trp substitutions at β85 were made and expressed in yeast in an effort to evaluate the role of Phe‐β85 in the acceptor pocket during polymerization of deoxy Hb S. The four Hb S variants have the same electrophoretic mobility as Hb S, and th