Respiratory 6: Transport of O2 and CO2 Flashcards
Where is haemoglobin blood.
It is kept in a RBC, because it can be concentrated without affecting viscosity of the blood.
What are the ways that O2 is transported in blood and which is the majority
- Binds with haemoglobin (majority)
2. Dissolves in solution
How does haemoglobin molecule bind O2
Haemoglobin has an 4 x a and B polypeptide chains containing a haem (fe2+) moiety in a chain.
The binding of O2 has cooperative allosteric effect where it twists the haem moiety to make next site more exposed to O2 for binding. (Speeds up as more O2 binds)
What does the Oxygen dissociation curve tell us about the binding of haemoglobin. What are the main features of the graph
Main features :
% oxygen saturation: (4 O2 = 100%) on the y. and partial pressure of O2 on the x.
There is a sigmoidal relationship due to cooperative binding
In the systemic veins, what is the PO2 and what does this mean for saturation of Haem compared to when its in the systemic arteries.
In Systemic veins the PO2 is low: 40 mmHg. This means that Haem has less affinity to take up O2. This encourages release
In the Systemic arteries/ alveoli
PO2 is high: 100 mmHG.
This means haem has higher affinity for binding O2.
This encourages O2 uptake
Why does Hb Affinity for O2 change as you go from Lungs to Veins
The tissues are more acidic because there is more CO2 going to Carbonic acid-> H+. This means that Hb has less affinity.
Whereas at lungs there is less CO2, so higher pH and O2 and is taken up and its max affinity restored.
What is the ratio of Carbon dioxide transported as bicarbonate in the plasma vs in red blood cells.
Where does the majority of bicarbonate come from in plasma vs RBC
70% transported in plasma to 30% RBC
- Majority of the bicarbonate in plasma (60%) has originated from the RBC by help of enzyme then diffused out.
- Majority in RBC (20%) is the rapidly forming bicarbonate
What is the difference between saturation and content of oxygen in blood
Saturation refers to the amount of O2 that the Hb can carry (1-4). It is not affected by volume of blood.
However the content of oxygen in the blood is affected by the amount of Hb present (volume of blood) and the saturation of that Hb as well.
What is the Bohr shift and what causes it
This is a shift in the oxygen dissociation curve to the right, meaning that Hb’s affinity for O2 is reduced for the same PO2, therefore promoting O2 release.
This is caused by increased metabolism products (at tissues)
: CO2, [H+] DPG, temperature.
What is the “opposite” Bohr shift and what causes it
This is a shift of the oxygen disassociation curve to the left, meaning the affinity for O2 is increased for the same PO2.
It is caused by : Decreased CO2, [H+], temperature, DPG. By making the Haem hs a higher affinity for O2. This sigmoidal relationship is moving depends on location of RBC
What shift does Fetal haemoglobin have on the oxygen dissociation curve and why is this important
Shift is to the left because it has higher affinity per PO2. This is important to help move O2 across the placenta from the mother’s haemoglobin to the foetus.
What shift does Myoglobin have on the oxygen dissociation curve and why is this important
It has big shift to the left, meaning that it has high affinity for O2 over a large range of PO2 and it only rlly dissociates when PO2 is really low so its a good storage of O2 for muscle.
What are the ways that CO2 is transported in blood - by most to least
- Transported mainly in HCO3- (bicarbonate)
- Combines to amine groups (on the heme molecule)
- CO2 is dissolved in solution
- Transported as H2CO3 and Co3- ions
(CO2 20x more soluble than O2 in blood )
How bicarbonate formed and what is the difference between rapidly and slowly forming.
CO2 + H2O is the limiting step -> forming carbonic acid which dissociates into bicarbonate and H+.
Rate limiting step makes rapid with carbonic anhydrase (in RBC) or slow without it.
How does CO2 associate with amine groups on Hb
CO2 + R-NH2 -> R- NHCOO- + H+
Amine group loses an H to let COO join on.