Explanation:
From the graph, 70% saturation corresponds with a partial pressure of 40 mm Hg.
The classic sigmoidal oxygen disassociation curve shows haemoglobin’s percentage saturation at different oxygen concentrations (partial pressures). This shows the equilibrium between oxyhaemoglobin (haemoglobin in its oxygen bound state and haemoglobin (free of oxygen molecules). The saturation generally increases with increased partial pressures of oxygen.
Further Explanation:
Haemoglobin is an oxygen binding protein comprising four iron-based peptide subunits: two α subunits and two β subunits. Each molecule of haemoglobin has the ability to bind up to four oxygen molecules at a time; this occurs via cooperative binding- meaning that with increased haemoglobin- oxygen binding at the protein haemoglobin’s subunits,(where oxygen is a ligand) there is an increase in its affinity for oxygen.
This is because there is a conformational change in the hemoglobin molecule due to the altered orientation of the protein’s secondary structures, making it easier for a second molecule of oxygen to successively followed by more O2-Haem binding until the molecule is saturated- at this point the curve plateaus- it reached its carrying limit.
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