Hemoglobin Athens-Georgia, or alpha 2 beta 2 40(C6)Arg replaced by Lys, a hemoglobin variant with an increased oxygen affinity.
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that of hemoglobin-A. Arginyl residue in position 40 of the beta chain, corresponding to position 6 of the C helix, has been replaced by a lysyl residue. This amino acid substitution is at the alpha1-beta2 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.
D000293:Adolescent; D000328:Adult; D000595:Amino Acid Sequence; D001120:Arginine; D005260:Female; D014644:Genetic Variation; D006454:Hemoglobins; D006455:Hemoglobins, Abnormal; D006801:Humans; D006863:Hydrogen-Ion Concentration; D008239:Lysine; D008297:Male; D008875:Middle Aged; D010100:Oxygen / Q000097:blood*; D010313:Partial Pressure; D010375:Pedigree
D006454:Hemoglobins; D006455:Hemoglobins, Abnormal; D001120:Arginine; D008239:Lysine; D010100:Oxygen