Hemoglobin Fort Gordon or alpha2beta2145 Tyr replaced by Asp, a new high-oxygen-affinity hemoglobin variant.
Hemoglobin Fort Gordon, alpha2beta2145 Tyr replaced by Asp (HC2), has been observed in a 20-year-old black male with compensatory erythrocytosis. The variant was readily identified by electrophoresis and chromatography, and comprised about 30% of the red cell hemoglobin. The substitution was identified through analyses of tryptic peptides of various digests of the isolated beta chain. The oxygen affinity of whole blood was increased; two components were observed one of which had a greatly increased affinity for oxygen and a markedly reduced subunit cooperativity. It appears that the Tyr replaced by Asp substitution resembles the Tyr replaced by His substitution in hemoglobin Bethesda (Bunn, H. F. et al. (1972) J. Clin. Invest. 51, 2299-2309; Olson, J. S. and Gibson, G. H. (1972) J Biol. Chem. 247, 3662-3670; Adamson et al. (1972) J. Clin. Invest. 51, 2883-2888) in that both inhibit the quarternary change of the oxy to the deoxy conformation, resulting in greatly altered functional properties. Studies of a few members of the family were negative.
D000328:Adult; D000595:Amino Acid Sequence; D001224:Aspartic Acid / Q000032:analysis; D014644:Genetic Variation; D005845:Georgia; D006455:Hemoglobins, Abnormal / Q000032:analysis; D006801:Humans; D007700:Kinetics; D008297:Male; D010100:Oxygen / Q000097:blood*; D010313:Partial Pressure; D010446:Peptide Fragments / Q000032:analysis; D014443:Tyrosine / Q000032:analysis
D006455:Hemoglobins, Abnormal; D010446:Peptide Fragments; D001224:Aspartic Acid; D014443:Tyrosine; D010100:Oxygen