Oxygen-Binding Properties for Hb βG16D, K120E, and Hb βC112D
Hemoglobin . | P50 . | n50 2, 3-BPG (−) . | |
---|---|---|---|
2, 3-BPG (−) . | 2, 3-BPG (+) . | ||
Hb A | 3.7 | 13.5 | 2.74 |
Hb βG16D, K120E | 3.6 | 11.4 | 2.74 |
Hb βC112D | 2.2 | 10.3 | 2.60 |
Hemoglobin . | P50 . | n50 2, 3-BPG (−) . | |
---|---|---|---|
2, 3-BPG (−) . | 2, 3-BPG (+) . | ||
Hb A | 3.7 | 13.5 | 2.74 |
Hb βG16D, K120E | 3.6 | 11.4 | 2.74 |
Hb βC112D | 2.2 | 10.3 | 2.60 |
Oxygen equilibrium curves of Hb A, Hb βG16D, K120E, and Hb βC112D were determined in 50 mmol/L Bis Tris buffer, pH 7.1 containing 0.1 mol/L NaCl at 20°C. P50 is the partial oxygen pressure required to give 50% oxygen saturation of hemoglobin. n50 values were calculated from the Hill plot of oxygen equilibrium curves. Concentration of 2, 3-BPG when present (+) is 2 mmol/L.