title: Hemoglobin Hotel-Dieu beta 99 Asp replaced by Gly (g1). A new abnormal hemoglobin with high oxygen affinity.
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 beta chain. As in other abnormal hemoglobins in which substitution of this residue has occurred, Hb Hotel-Dieu exhibits a high oxygen affinity and is associated with familial erythrocytosis.
mesh_terms: D000328:Adult; D000596:Amino Acids / Q000032:analysis; D005260:Female; D014644:Genetic Variation; D006454:Hemoglobins / Q000032:analysis; D006455:Hemoglobins, Abnormal / Q000302:isolation & purification / Q000378:metabolism*; D006801:Humans; D008297:Male; D010100:Oxygen / Q000097:blood; D010375:Pedigree; D010446:Peptide Fragments; D011086:Polycythemia / Q000097:blood*
chemical_list: D000596:Amino Acids; D006454:Hemoglobins; D006455:Hemoglobins, Abnormal; D010446:Peptide Fragments; C028905:hemoglobin Hotel-Dieu; D010100:Oxygen