How is foetal haemoglobin adapted to increase aerobic respiration and prevent anaerobic respiration?
It has a high affinity for O2 meaning it can obtain oxygen via the placenta allowing aerobic respiration and preventing anaerobic respiration causing a shift to the left.
How is myoglobin adapted to increase aerobic respiration and prevent anaerobic respiration?
Myoglobin is a store of oxygen so it only dissociates from O2 in very low PO2s therefore it maintains aerobic respiration and prevents anaerobic respiration causing a shift to the left.
They have a relatively large surface area to volume ratio so loose thermal energy quickly meaning they have to aerobically respire at a higher rate meaning the haemoglobin dissociates with O2 more often causing a Bohr shift.
How do animals with high activity levels adapt to survive?
Their tissues require plenty of oxygen to maintain aerobic respiration so Haemoglobin has to be able to easily dissociate. This causes the Bohr shift which is an advantage as the small decrease of PO2 will cause a large dissociation of O2 therefore can maintain a high rate of aerobic respiration and prevent anaerobic respiration.
How do organisms adapt to environments with low oxygen?
Haemoglobin has to be good at loading oxygen in lower PO2s (the curve would move to the left). The advantage of this position is that haemoglobin is fully saturated even in lower PO2s therefore allowing aerobic respiration and preventing anaerobic respiration.
By creating a lower Hb % saturation of O2 there will be a lower affinity between Hb and O2 so it is more likely to dissociate to maintain aerobic respiration and prevent anaerobic respiration
What happens when the 4O2 leaves the red blood cell?
It releases oxygen as it dissociates from haemoglobin where it moves into respiring cells as there is a lower PO2 for aerobic respiration to occur and to prevent anaerobic respiration.
Section C model answer of the haemoglobin sigmoid curve
When PO2 starts to increase from very low PO2 the first O2 that associates with haemoglobin causes a change in the quaternary structure. This exposes all 3 haem groups making it easier for O2 to associate. This leads to rapid increase in percentage saturation.
1. What is happening to the PO2 - (There is a high PO2 in the lungs)2. How is there affinity to O2 - (therefore haemoglobin has a high affinity for O2)3.Does O2 associate or dissociate - (therefore haemoglobin is more likely to associate with O2)4.Finish the scenario - (allowing haemoglobin to become fully saturated with O2)