Haemoglobin Flashcards
Definition of:
1) Affinity
2) Saturation
3) Loading/Unloading
1) Natural attraction to something
2) How much O2 is combined with haemoglobin
3) When O2 is taken up/released
How to calculate percentage saturation of haemoglobin with oxygen?
Oxygenated Haemoglobin
————————————— x100
Maximum Saturation
Names of axis on dissociation curve?
- Percentage saturation of haemoglobin to oxygen (%)
- Partial pressure of oxygen (KPa)
Explain how oxygen is loaded, transported + unloaded in the blood? (6)
- Haemoglobin carries oxygen/ high affinity for O2
- In red blood cells
- Loading in the lungs
- At high partial pressure of O2
- Unloads to respiring tissues
- At low partial pressure
The oxygen dissociation curve of the foetus is to the left of its mother.
Explain the advantage of this for the foetus? (3)
- Higher affinity/loads more oxygen
- At low/same partial pressure
- Oxygen moves from mother to foetus
Heat from respiration helps mammals to maintain a constant body temperature.
Use the information to explain the relationship between the surface area:volume ratio of mammals + the oxygen dissociation curves of their haemoglobin? (5)
- Smaller mammal gas greater surface area to volume ratio
- So more heat is lost
- So has greater rate of respiration/metabolism
- Oxygen required for aerobic respiration
- Haemoglobin releases more oxygen/ haemoglobin has lower affinity
Describe how haemoglobin normally loads oxygen in the lungs + unloads it in a tissue cell? (6)
- Oxygen combines to produce oxyhemoglobin
- Each haemoglobin molecule may transport 4 molecules of O2
- High partial pressure of oxygen in lungs so high saturation
- Presence of CO2 increases oxygen dissociation
- So more O2 unloaded
- Low partial pressure/ increase CO2 in respiring tissue
Explain how oxygen in red blood cells is made available for respiration in active tissues? (4)
- CO2 increased respiration
- So increases dissociation of oxygen from haemoglobin
- Low partial pressure in tissues
- Oxygen diffuses from r.b.c. to tissues
Explain why binding of one molecule of oxygen to haemoglobin makes it easier for a second oxygen molecules to bind? (2)
- Binding of first oxygen changes tertiary/quaternary structure of haemoglobin
- Which uncovers another binding site
Describe + explain the effect of increasing CO2 conc. on the dissociation of oxyhemoglobin? (2)
- Increases unloading/ decreases haemoglobin’s affinity for O2
- By decreasing blood pH
If the dissociation cure is to the left then… (3)
- Loads more oxygen
- At a lower partial pressure
- Haemoglobin has higher affinity for O2
If the dissociation curve is to the right then… (5)
- Loads less oxygen
- For more aerobic respiration so more ATP
- More heat energy released
- At the same partial pressure
- Haemoglobin has lower affinity for O2
In oxygen dissociation curve, if higher partial pressure of CO2 then…
- Saturation of haemoglobin decreases
- Curve shifts to the right as affinity for O2 is lower