Functional studies of two new abnormal hemoglobins with their mutation located at intersubunit contacts: Hb Hotel Dieu beta99 (G1) Asp replaced by Gly and Hb Pitie Salpetriere beta34 (B16) Val replaced by Phe.
The functional properties of two new abnormal hemoglobins with high oxygen affinity were studied. Hb Hôtel Dieu beta99 (G1) Asp replaced by Gly is situated in the alpha1beta2 contact. Hb Pitié Salpétrière beta34 (B16) Val replaced by Phe is situated in the alpha1beta1 contact. Both hemoglobins exhibited similar functional properties with a 10-fold increased oxygen affinity, a decreased cooperativity, a decreased Bohr effect and a normal or slightly decreased 2,3-diphosphoglycerate effect. The structure-function relationship is discussed in the light of these results.
D019794:2,3-Diphosphoglycerate; D000595:Amino Acid Sequence; D001224:Aspartic Acid; D004163:Diphosphoglyceric Acids / Q000097:blood; D005998:Glycine; D006455:Hemoglobins, Abnormal / Q000378:metabolism*; D006801:Humans; D006863:Hydrogen-Ion Concentration; D007525:Isoelectric Focusing; D010100:Oxygen / Q000097:blood; D010649:Phenylalanine; D013438:Sulfhydryl Compounds / Q000378:metabolism; D014633:Valine
D004163:Diphosphoglyceric Acids; D006455:Hemoglobins, Abnormal; D013438:Sulfhydryl Compounds; D019794:2,3-Diphosphoglycerate; D001224:Aspartic Acid; D010649:Phenylalanine; C032380:hemoglobin Pitie Salpetriere; C028905:hemoglobin Hotel-Dieu; D014633:Valine; D010100:Oxygen; D005998:Glycine