Abstract
Summary Hemoglobin Deaconess was detected as a band migrating in the position of fetal hemoglobin when an hemolyzate was electrophoresed on cellulose acetate at pH 8.4. This abnormal hemoglobin also migrates between Hb S and C on citrate agar electrophoresis at pH 6.2. Chemical characterization of this mutant hemoglobin shows glutamine is deleted at position 131 in the β-chain. Initial data indicates that the stripped hemoglobin has a reduced oxygen affinity with a Hill constant of n=2.0.
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