Abstract
HAEMOGLOBIN Seattle is a mutant displaying a considerable decrease in oxygen affinity with almost normal haem-haem interaction and normal Bohr effect1. Structural studies have indicated that the chemical abnormality in this mutant is a substitution of alanine by glutamic acid in tryptic peptide βTp9. This peptide includes residues 67 to 82 of the β chain with alanines occupying positions 70 and 76. Structural analysis of the Seattle βTp8–9 and βTp9 using the Edman degradation and exopeptidase digestion suggested that the substitution was located at residue 76β. Therefore, it was concluded that the structure of Hb Seattle was 76β alanines→glutamic acid2.
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