Gas transport Flashcards
- State Dalton’s Law.
Partial pressure in a gas mix is the sum of the partial pressure of each of the gases
- State Fick’s Law.
Molecules diffuse from regions of high conc to low conc in a rate proportional to the gradient, surface area and diffusion capacity of the gas, but inversely proportional to thickness
- State Henry’s Law.
At constant temp, the amount of gas that will dissolve is directly proportional to its partial pressure
- State Boyle’s Law.
Volume is inversely proportional to pressure
- State Charles’ Law.
Volume is proportional to temperature
- Describe how partial pressure of oxygen changes as it passes down the airways.
Partial pressure of o2 starts around 21.3kPa, 0Co2 and 0h20
As it goes down air gets humidified, slowed and mixed-20kPa O2, OCo2 and 6.3h20. In the resp airway, O213.5, Co2 5.3 and H2O 6.3
- What happens to the air as it passes down the airways?
It gets humidified, warmed, slower and mixed
- How much oxygen can be dissolved in our blood?
Blood cannot take much oxygen-17ml of O2 can be dissolved in ALL our blood at 0.34ml/dL. Whats needed for life is 250ml/min so not even close
- What is the normal oxygen consumption at rest?
250ml/min
- What is the binding capacity of oxygen to haemoglobin?
That why we use haemoglobin-can carry a lot more oxygen than just blood. 2% is dissolved, 98 is haemoglobin 15.1ml/dL
- Describe the structure of a normal variant of haemoglobin and of foetal haemoglobin.
Fe2+ in heam group binds 1 O2 each
Haemoglobin is a 2 alpha 2 beta tetramer-that’s haemoglobin A (HbA). Normal variant HbA2 exists with 2alpha and 2delta-2% of Hb
Foetal haemoglobin, HbF is 2 alpha and 2 gamma (trace)
- Explain why haemoglobin is considered an ‘allosteric’ molecule.
Oxygen affinity is actually low if none is bound. But as the 1st one bind, conformational change which increases affinity-and as more bind, the more the affinity increase. So low affinity for 1st one but high for the 4th one
- What change occurs in the middle of the haemoglobin tetramer when oxygen binds?
As it binds O2, space for 2,3DPG to bind appears-which reduces affinity for O2. 2,3DPG is a by product of glycolysis, so as/where ATP metabolism is high, the DPG comes in and SQUEEZE out the last few O2 molecules
- What is the name given to the phenomenon where oxygen binding to haemoglobin increases the affinity making more oxygen bind?
Cooperative bindin-results in a sigmoidal binding curve of O2 in relation to conc/pressure
- What would the consequences be if the oxygen dissociation curve was linear?
Youd get a very large saturation change/variance in the lungs, where the pressure differs-very little scope to purely load
- What are the benefits of having a sigmoid ODC?
Large variation of saturation in tissue, at low pO2. But as the pressure is high (lungs) the saturation is very high and stays all throughout the change of pressure-near 100% saturation at alveaolar pO2, but goes fro, 8% to 76% in tissue pO2
- What is P50?
The pressure at which 50% of oxygen is saturated-normally in range with tissue pO2, but can give a good idea of where the curve is (right shifted , left shifter). Normaly around 3.3kPa
- What conditions can shift the ODC to the right?
Right shift reflects a higher energy consumption-exercise. Along that happens increase in temp, acidosis, Hypercania (high CO2), increase 2,3DPG)-oxygen is dissociating MORE in tissue, so has less saturation as it exits those lower tissue pressure (around 50% vs 76% before)
- What conditions can shift the ODC to the left?
The opposite to exercise-oxygen dissociates LESS-comes out of tissue more saturated. Happens with decrease of temp, alkalosis, hypocapnia, Decrease 2,3DPG
- What conditions can shift the ODC upwards?
means you can just carry MORE oxygen-the 100% saturation now corresponds to a higher amount of O2 in blood. Due to polycynthaemia-increase of haematocrit due to increase RBC. Saturation as exit tissue the SAME, as it has still unloaded the right amount of O2
- What conditions can shift the ODC downwards?
Downwards means you can carry LESS oxygen-aneamia, or lack of Fe2+ is a common one. As you unload the same amount of O2 in tissue, saturation is the SAME
- How does haemoglobin saturation change in the previous two shifts (up and down) of the ODC?
Curve are shifter up/down but the Y axis is also adjusted-what changes isn’t the % of total, but the actual total being higher/lower
- How does carbon monoxide shift the ODC and why?
CO has much greater affinity-meaning it bind Hb better than O2. So it reduces how much O2 you can carry and the Max O2 saturation you can have. It increases affinity by cooperative binding, but decreases capacity (down and left shift)
- Describe the shape of the ODC of myoglobin and foetal haemoglobin and why this shape is needed for their function.
Myoglobin is a monomeric muscle protein with a sigmoidal binding curve. At the same pressure of O2, it is much more saturated, meaning its affinity for O2 is higher-steals it from HbA to provide muscle
Foetal haemoglobin is similar, to give O2 to child-but still sigmoidal, just higher. Higher affinity for O2 at same pressure than HbA