Abstract
A new hemoglobin variant, termed hemoglobin Athens-Georgia, has been found in a 23-year-old Caucasian student and three members of her family. The electrophoretic mobility of this variant at pH 9.0 is slightly less than that of hemoglobin-A. Arginyl residue in position 40 of the β chain, corresponding to position 6 of the C helix, has been replaced by a lysyl residue. This amino acid substitution is at the α 1- β 2 contact and slightly affects the oxygen binding properties of the hemoglobin molecule. Hemoglobin Athens-Georgia has an increased affinity for oxygen, a normal heme-heme interaction and a normal Bohr effect. Hematological abnormalities are not associated with this variant.
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Schedule a callMore From: Biochimica et Biophysica Acta (BBA) - Protein Structure
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