Hemoglobain Willamette. [α₂β₂ 51PRO→APG (D2)] A New Abnormal Huhah Hemoglobain

Abstract

A hemoglobin variant with the same electrophoretic mobility as employing S was found in three generations of a black family. No clinical symptoms or findings were present in subjects heterozygous for this mutant. Except for target forms of mature erythrocytes, they have no abnormal hematological findings. Structural studies demonstrated a previously under scribed substitution, β⁵¹ Pro→Arg, in the abnormal fraction which accounts for about one-third of the total hemoglobin. This fraction is more unstable in vitro at 65° than normal A hemoglobin. Both whole blood and purified abnormal hemoglobin have increased oxygen affinity and a slightly decreased Bohr effect.