Transport of Oxygen
Haemoglobin
Transported in erythrocytes (red blood cells)
Associates with oxygen to form oxyhaemoglobin (Hb(CO₂)₄)
Consists of 4 polypeptide chains in a quaternary structure
Each chain consists of a non-protein haem group each containing an iron ion (Fe2+)
which attracts and holds oxygen molecules
Haemoglobin has a high affinity for oxygen
Oxygen dissociates and leaves haemoglobin to be released into respiring tissues
Partial Pressure of Oxygen
Oxygen tension = oxygen concentration
Also called partial pressure of oxygen (pO₂) and measured in kilopascals (kPa)
Oxygen has a long diffusion distance to the haem group
Low pO₂ = low saturation
After one O₂ molecule binds to a haem group, a conformational change occurs in the
haemoglobin molecule
The shape changes and the haem groups move to the outside
Allows O₂ molecules to associate with ease
Approaching 100% saturation, diffusion gradient decreases and oxygen struggles to
associate
After birth there is a change in environment to higher oxygen tension so adult haemoglobin is
different to foetal haemoglobin so dissociation can occur
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