All of the factors are responsible for unloading of oxygen from the hemoglobin molecule except the increase in partial pressure of oxygen.
Because the affinity of haemoglobin for binding oxygen increases as partial pressure of oxygen rises.
<h3>What is Haemoglobin?</h3>
Red blood cells include the protein hemoglobin, which transports oxygen to your body's organs and tissues and carbon dioxide from those tissues back to your lungs.
<h3>What are factors that affect Haemoglobin's affinity for oxygen?</h3>
When used as an oxygen transporter, hemoglobin can carry about 65 times as much oxygen as simple solution in plasma could.
A cooperative oxygen-hemoglobin affinity is produced by conformational changes in the molecule.
The oxygen-hemoglobin dissociation curve's sigmoidal form reflects this characteristic.
Temperature, hydrogen ions, carbon dioxide, and intraerythrocytic 2,3-DPG all have an impact on hemoglobin's affinity, and they all interact with one another.
