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Abstract
Hb Iowa with a Gly→Ala mutation at position β119(GH2) was observed in a Black infant and her mother. The baby was also heterozygous for Hb S; Hb Iowa was confused with Hb F at birth because its electrophoretic mobility was similar to that of Hb F1. The β chain of Hb Iowa could be readily separated from the βA, α, and γ chains by polyacrylamide gel electrophoresis and by reversed phase high performance liquid chromatography. Structural characterization was through amino acid analyses of peptides isolated from a tryptic digest of the aminoethylated β-Iowa chain. The Gly→Ala replacement in Hb Iowa does not affect its stability and oxygen carrying properties; hematological data for mother and child were within normal ranges.