1
Q
describe the structure of haemoglobin
A
- a globular protein with a quaternary structure
- 4 polypeptide chains
- 4 haem groups each with an ion of iron
- 1 molecule binds to 4 oxygens as they each bind to a haem group
2
Q
give the adapations of red blood cells
A
- bi concave disc to increase surface area
- no nucleus which increases storage room for oxygen
3
Q
desribe what happens at the lungs
A
- there is a high partial pressure of oxygen at the lungs
- therefore more oxygen can bind to the haemoglobin and associate as the haemoglobin will have a higher affinity for oxygen
- this is also known as the loading of oxygen
4
Q
what happens at the respiring cells/tissue
A
- there is a low partial pressure of oxygen in the respiring cells
- therefore haemoglobin has a lower affinity for oxygen and it will dissociate
- this is also known as the unloading of oxygen
5
Q
what is the difference between fetal haemoglobin and adult haemoglobin
A
fetal blood has a higher affinity for oxygen and so this ensures that the fetus gets enough oxygen for development
the haemoglobin in the mothers blood has a lower affinity for oxygen which allows oxygen to dissociate and bind to the fetal haemoglobin
6
Q
explain the Bohr effect
A
