Myoglobin, oxygen saturation curve

Figure 2.19 Oxygen saturation curves for myoglobin and haemoglobin and different pH values. (Reproduced by permission of John Wiley Sons, Ltd).

Figure 2-13. Oxygen saturation curves for myoglobin and adult hemoglobin (HbA). Myoglobin has a hyperbolic saturation curve. HbA has a sigmoidal curve. The HbA curve shifts to the right at lower pH, with higher concentrations of 2,3-bisphosphoglycerate (BPG), or as C02 binds in the tissues. Thus, 02 is released more readily. P50 ( ) is the partial pressure of 02 at which HbA is half-saturated with 02.

Figure 1-1. Oxygen saturation curves for hemoglobin and myoglobin.

Rg. 2 Comparison of oxygen saturation curves for haemoglobin and myoglobin. 

FIGURE 4.25 The oxygen saturation curves for myoglobin and for hemoglobin at five different pH values. 

Oxygen binding curves of myoglobin and hemoglobin. Note the reduced hemoglobin saturation at low oxygen pressure that allows better delivery of oxygen to peripheral tissues. 

Myoglobin saturation curve. The saturation of myoglobin is shown as a function of oxygen concentration. 

For hemoglobin, n 2.8 (sigmoidal saturation curve), and for myoglobin, n = 1 (hyperbolic saturation curve). The efficiency of O2 transfer from hemoglobin to myoglobin is further enhanced by a decrease in pH since oxygen binding is pH-dependent (the Bohr effect). 

Fig. 13. Typical oxygen equilibrium curves for haemoglobin (curve a) and myoglobin (curve b) curve c indicates a myoglobin-type (i.e., a non-cooperative oxygenation curve) with the same percentage saturation as haemoglobin at venous oxygen partial pressure.

FIGURE 9.18 The variation of the extent of saturation of myoglobin (Mb) and hemoglobin (Hbl with the partial pressure of oxygen. The different shapes of the curves account for the different biological functions of the two proteins. 

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