Oxygen dissociation curve myoglobin

THE OXYGEN DISSOCIATION CURVES FOR MYOGLOBIN HEMOGLOBIN SUIT THEIR PHYSIOLOGIC ROLES... 

Hyperbolic shape of the enzyme kinetics curve Most enzymes show Michaelis-Menten kinetics (see p. 58), in which the plot of initial reaction velocity, v0, against substrate concentration [S], is hyperbolic (similar in shape to that of the oxygen-dissociation curve of myoglobin, see p. 29). In contrast, allosteric enzymes frequently show a sigmoidal curve (see p. 62) that is similar in shape to the oxygen-dissociation curve of hemoglobin (see p. 29). 

Figure 25.8 Oxygen dissociation curves for haemoglobin and myoglobin, showing how haemoglobin is able to absorb O2 efficiently in the lungs yet transfer it to myoglobin in muscle tissue.

Figure 25.1 Oxygen dissociation curves for myoglobin (A) and haemoglobin at Pcoj values of 40 mmHg(B) and 80 mmHg (C)...

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