Haemoglobin Flashcards
What is haemoglobin?
A large protein with a quaternary structure: it is 4 polypeptide chains and 4 iron ion prosthetic groups which travels in blood to carry oxygen
Structure of haemoglobin
4 polypeptide chains
2 alpha glob in 2 beta globin
4 iron haem groups
Where does oxygen bind to in haemoglobin?
4 iron prosthetic groups
Loading and unloading of oxygen to haemoglobin
Haemoglobin + 4 oxygen to form oxy haemoglobin
A reversible reaction so oxy haemoglobin can unload all 4 oxygen
Loading
Oxygen binds to iron in haemoglobin
Unloading
Oxygen unbinds from oxyhaemoglobin
What does the loading of oxygen onto haemoglobin depend upon?
The affinity haemoglobin has for oxygen
What affects the affinity haemoglobin has to oxygen?
The partial pressure of oxygen in the area
Trend for oxygen loading onto haemoglobin
Where there is a high partial pressure for oxygen, oxygen will unload onto haemoglobin more so higher affinity
So haemoglobin has a high % saturation to oxygen
Where does oxygen mostly load onto haemoglobin?
In the alveoli in the lungs because a high partial pressure of oxygen
Oxygen diffuses into blood from alveoli into blood
Trend for oxygen unloading from haemoglobin
Where there is a low partial pressure for oxygen, oxygen will unload from haemoglobin
So less affinity
And lower % saturation of haemoglobin with oxygen
Where does oxygen unload from haemoglobin?
In respiring tissues where oxygen has been used in respiration so has a low partial pressure of oxygen into cells
Affinity for oxygen in lungs
High
Affinity for oxygen in respiring tissues
Low
Partial pressure of oxygen
A measure of oxygen concentration in a given volume caused by oxygen molecules colliding which exerts pressure