Module 3 Section 2 : Haemoglobin Flashcards
Red blood cells contain…
Haemoglobin
What is haemoglobin
- A large protein with a quaternary structure - made up of one or more polypeptide chain (four of them)
- Each chain has a haem group which contains iron and gives haemoglobin its red colour
- Haemoglobin has a high affinity for oxygen each molecule can carry four oxygen molecules
How is oxyhemoglobin formed
- joins in the lungs
- oxygen joins to the iron in haemoglobin to form oxyhemoglobin
- reversible reaction - when oxygen leaves oxyhemoglobin near the body cells it turns back to haemoglobin
What is the word equation for how oxyhemoglobin is formed
Haemoglobin (Hb) + Oxygen (4O2) = oxyhemoglobin (HbO8)
What does haemoglobin saturation depend on
The partial pressure of oxygen
What is partial pressure of oxygen
- Partial pressure of oxygen is a measure of oxygen concentration
- the greater the concentration of dissolved oxygen in cell, the higher the partial pressure
What is the symbol of partial pressure of oxygen
pO2
What is the partial pressure of Carbon dioxide
- the partial pressure of carbon dioxide is a measure of concentration of CO2 in a cell
- the greater the concentration of dissolved carbon dioxide in cells the higher the pressure
Haemoglobins affinity for oxygen varies depending on…..
Partial pressure of oxygen:
Oxygen loads into haemoglobin to form oxyhaemoglobin where there’s a high pO2
Oxyhaemoglobin disassociates it’s oxygen where there’s a lower pO2
Give a situation when oxygen loads into haemoglobin
When oxygen enters blood capillaries at the alveoli in the lungs. Alveoli have a high pO2 so oxygen loads into haemoglobin to form oxyhemoglobin
Give a situation when oxygen disassociates from oxyhemoglobin
When cells respire they use up oxygen - this is a lower pO2. Red blood cells deliver oxyhemoglobin to respiring tissues where it disassociates its oxygen
After disassociation what happens to the haemoglobin
The haemoglobin then returns to the lungs to pick up more oxygen
What shows how saturated the haemoglobin is with oxygen at any given partial pressure
An oxygen dissociation curve
Where the pO2 is high haemoglobin has….
A high affinity for oxygen (it will readily combine with oxygen), so it has a high saturation of oxygen
Where pO2 is low haemoglobin has a….
Low affinity for oxygen which means it releases oxygen rather than combines with it. That’s why it has a low saturation of oxygen.
Why is the oxygen dissociation curve an s-shape
- Because when haemoglobin combines with the first O2 molecule it’s shape alters in a way that makes it easier for other molecules to join too.
- But as Hb starts to become saturated, it gets harder for more oxygen molecule to join
- the curve has a steep bit in the middle where it’s really easy for oxygen molecules to join
- the curve has shallow bits at each end where it’s harder for oxygen molecules to join.
What is the meaning when the curve is steep
When the curve is steep a small change in pO2 causes a big change in the amount of oxygen carried by Hb
What has a higher affinity for oxygen Fetal haemoglobin or adult haemoglobin
Fetal haemoglobin has a higher affinity for oxygen than adult haemoglobin
Why does Fetal haemoglobin have a higher affinity for oxygen than adult haemoglobin
Fetal haemoglobin has a higher affinity for oxygen because the fetus’s blood is better at absorbing oxygen than it’s mothers blood at the same partial pressure of oxygen
How does a fetus get oxygen from its mothers blood
Across the placenta
What happens to the oxygen saturation by the time the blood reaches the placenta
It has decreased by the time it reaches the placenta. This is because some has been used up by the mother’s body
Why does a fetus need to have a higher affinity for oxygen
It needs a higher affinity because the fetus needs to get enough oxygen to survive
What would happen if Fetal haemoglobin had the same affinity for oxygen as adult haemoglobin
If the Fetal haemoglobin had the same affinity for oxygen as adult haemoglobin it’s blood wouldn’t be saturated enough
What affects oxygen unloading
Carbon dioxide concentration
When does haemoglobin give up its oxygen more readily and why does it happen
- At higher partial pressures of carbon dioxide (pCO2)
Where does most of the CO2 diffuse into
Most of the CO2 from the respiring tissues diffuses into red blood cells
What does the CO2 react with, produce and what is it catalysed by
- Reacts with water
- Forms Carbonic acid
- Catalysed by the enzyme carbonic anhydrase
- the rest of the CO2, around 10% binds directly to haemoglobin and is carried to the lungs
What happens to carbonic acid after it’s formed
The carbonic acid dissociates (splits up) to give hydrogen (H+) ions and hydrogencarbonate (HCO3-) ions
What does the increase in H+ ions cause
- This increase in H+ ions causes oxyhemoglobin to unload its oxygen so that haemoglobin can take up the H+ ions
- This forms a compound called Haemoglobinic acid.
- This process also stops the hydrogen ions from increasing the cell’s acidity
What happens to the hydrogencarbonate ions
The HCO 3- ions diffuse out of the red blood cells and are transported in the blood plasma
How does the red blood cells compensate from the loss of HCO3- ions
To compensate for the loss of HCO3- ions from the red blood cells, chloride (Cl-) ions diffuse into the red blood cells. This is called the chloride shift
What does the chloride shift do
The chloride shift maintains the balance of charge between the red blood cells and the plasma
What happens to the blood when it reaches the lungs
- The low pCO2 causes some of the HCO3- and H+ ions to recombine into CO2 (and water).
- The CO2 the diffuses into alveoli and is breathed out
What is the Bohr Effect
When carbon dioxide levels increase, the dissociation curve ‘shifts’ right showing that more oxygen is released from the blood (because the lower the saturation of haemoglobin with O2 the more O2 is released).
How does CO2 affect oxygen unloading
- Most CO2 from respiring tissues diffuses into red blood cells
- reacts with water to form carbonic acid
- which is catalysed by carbonic anhydrase
- carbonic acid dissociates to give hydrogen ions and hydrocarbonate ions
- increase in H+ cause oxyhemoglobin to unload its oxygen so Hb can take up the H+ ions
- hydrogencarbonate ions diffuse out of RBC and are transported in the blood plasma
- to compensate for loss is hydrogencarbonate ions in RBC, Cl ions diffuse into the RBC
- Called the chloride shift
- chloride shift maintains the balance of charge between RBC and the plasma
- When blood reaches lungs the low pCO2 causes some of the hydrogen carbonate and hydrogen ions to recombine into CO2
- the CO2 then diffuses into the alveoli and is breathed out