Case Study: Mutations In Hemoglobin and Their Effect on Oxygen Transport In vertebrates, hemoglobin, found in red blood cells, is responsible for the transport of oxygen. The functional form of hemoglobin is a tetramer. In human adults, almost all (>95%) of the hemoglobin is composed to two ” subunits and two β subunits (case. This form of hemoglobin is known as hemoglobin A (Hb A). Adults also carry a mino form known as hemoglobin A2 composed of two α subunits and two δ subunits (α2δ2 n a developing fetus the hemoglobin (Hemoglobin F) is composed of two a subunits and two γ subunits (α2/2). After birth the synthesis of the γ subunits decline, and the synthesis of the β subunits increase, leading to a decrease in hemoglobin F and an increase in hemoglobin A. In addition to these normal variants of hemoglobin there are several other forms of hemoglobin that are typically found in disease states. Hemoglobin C, composed of ß subunits containing the Glu6Lys mutation (apal Lys), Hemoglobin E composed of β subunits containing the Glu26Lys mutation (α2β2Gu26Lys), Hemoglobin S composed of β subunits containing the Glu6Val mutationß2Glub, and hemoglobin kempsey composed of β chains containing the Asp99Asn mutation (cr2B2Asp OA are examples of hemoglobin variants that cause disease. matab oo a acid CAaP Shown below if the oxygen saturation curve for Hb A and hemoglobin Kempsey. R ニ0.8 Hb/Kempsey to is Move stalow. 苗0.6 Hb A 0.4 0.2 0.0 0 2040 60 80100 P po2 (torr) Questions: Which hemoglobin has a higher affinity for oxygen? Justify your answer using estimates for the Pso value for Hemoglobin Kempsey and Hb A. kumpsey ha ighu afiy since wer psO 0″ Value s than HCA N36