Functional studies of two new abnormal hemoglobins with their mutation located at intersubunit contacts: Hb hotel dieu β99 (G1) Asp → Gly and Hb pitie salpetriere β34 (B16) Val → Phe

Abstract

The functional properties of two new abnormal hemoglobins with high oxygen affinity were studied. Hb Hôtel Dieu β99 (G1) Asp → Gly is situated in the α₁β₂ contact. Hb Pitié Salpétrière β34 (B16) Val → Phe is situated in the α₁β₁ 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.