Hemoglobin Hotel-Dieu β599 ASP → GLY (Gl). A New Abnormal Hemoglobin with high Oxygen Affinity

Y. Blouquit Unité de Recherches sur les Anémies INSERM U.91 and Laboratoire Central de Biochimie Höpital Henri Mondor, Créteil, 94010, France

F. Braconnier Unité de Recherches sur les Anémies INSERM U.91 and Laboratoire Central de Biochimie Höpital Henri Mondor, Créteil, 94010, France

F. Galacteros Unité de Recherches sur les Anémies INSERM U.91 and Laboratoire Central de Biochimie Höpital Henri Mondor, Créteil, 94010, France

N. Arous Unité de Recherches sur les Anémies INSERM U.91 and Laboratoire Central de Biochimie Höpital Henri Mondor, Créteil, 94010, France

J. Soria Service d'Hématologie - Hôtel-Dieu, Paris, 75004, France

R. Zittoun Unité de Recherches sur les Anémies INSERM U.91 and Laboratoire Central de Biochimie Höpital Henri Mondor, Créteil, 94010, France

J. Rosa Unité de Recherches sur les Anémies INSERM U.91 and Laboratoire Central de Biochimie Höpital Henri Mondor, Créteil, 94010, France

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Abstract

Hemoglobin Hotel-Dieu was detected by isoelectric focusing during investigation of a patient who had erythrocytosis. This variant migrates on cellulose acetate electrophoresis to a cathodic position relative to Hb F. In hemoglobin Hotel-Dieu, aspartic acid is substituted by glycine in position 99 of the β chain. As in other abnormal hemoglobins in which substitution of this residue has occured, Hb Hotel-Dieu exhibits a high oxygen affinity and is associated with familial erythrocytosis.

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Hemoglobin Hotel-Dieu β599 ASP → GLY (Gl). A New Abnormal Hemoglobin with high Oxygen Affinity

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Hemoglobin Hotel-Dieu β599 ASP → GLY (Gl). A New Abnormal Hemoglobin with high Oxygen Affinity

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