Solution for QID #3349: Properties of human hemoglobins Hb Structure P50* Hillt Bohr | StudyHelpMe

Properties of human hemoglobins Hb Structure P50* Hillt Bohrt 2,3-BPGS Gower-1 5262 1.4 + 0.06 1.7 + 0.24 -0.25 0.09 Gower-2 02E2 2.7 + 0.10 2.3 + 0.02 -0.51 0.17 Portland-2 52 B2 1.9 + 0.17 1.6 + 0.06 -0.10 0.30 A a2B2 3.2 + 0.14 2.9 + 0.36 -0.54 0.29 *torr; tlog(Y/1 - Y)/log PO2; Alog Pso/ApH in the alkaline region; Sapparent binding constant (mM) calculated from half-saturation point. Above are data from the paper Expression, purification, and characterization of human hemoglobins Gower-1, Gower-2, and Portland-2 assembled in complex transgenic-knockout mice by He and Russell (2001). Hemoglobin A is the wild-type, while Gower-1, -2 and Portland-2 are mutations to hemoglobin that affect the quaternary structure of hemoglobin which leads to distinct functional properties. Analyze the data and then answer the question. The "normal" hemoglobin is denoted as "A". The Bohr column refers to the change in p50 value with pH and the 2,3 BPG column is the Kp in mM for 2,3BPG binding to the hemoglobin. The Structure column is the subunit composition (a, B, (, E). Remember normal hemoglobin is a2 82