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Hemoglobin Malmö β-97 (FG-4) Histidine→Glutamine: A Cause of Polycythemia

Samuel H. Boyer, Samuel Charache, Virgil F. Fairbanks, Jorge E. Maldonado, Andrea Noyes and Esther E. Gayle

Department of Medicine, The Johns Hopkins University School of Medicine, Baltimore, Maryland 21205

Department of Laboratory Medicine, the Mayo Foundation, Rochester, Minnesota 55901

Department of Medicine, the Mayo Foundation, Rochester, Minnesota 55901

Published March 1972

A striking history of familial polycythemia led to a search for an abnormal hemoglobin. None could be demonstrated by routine electrophoretic methods, but the propositus' hemolysate had increased oxygen affinity. Manipulation of the conditions of electrophoresis, and chromatographic methods, permitted identification of hemoglobin Malmö. Studies of hemolysates demonstrated a normal Bohr effect, decreased heme-heme interaction (n=1.58), and a p50 of 1.3 mm Hg at 10°C and pH 7.2. The amino acid substitution occurs in the same position (FG-4) as that of hemoglobin Chesapeake, but in the β-chain rather than the α-chain. The two types of hemolysate have different pathophysiologic properties, and carriers of hemoglobin Malmö exhibit more striking hematologic abnormalities.


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