4 - Gas Transport and Exchange Flashcards
What are the following prefixes in nomenclature? P F S C Hb
P- partial pressure F - fraction S - Hb saturation C - content (mL) Hb - volume bound to Hb (mL)
name the 5 gas laws
- Dalton’s
- Fick’s
- Henry’s
- Boyle’s
- Charles’
what is Dalton’s law?
(partial pressures)
the partial pressure of gas in a mixture is equal to the sum of the partial pressure of gases in the mixture
What is Fick’s law?
(diffusion)
molecules diffuse from regions of high concentrations to low concentrations at a rate proportional to the concentration gradient, the exchange surface area and diffusion capacity of the gas, and inversely proportional to the thickness of the exchange surface
what is Henry’s Law?
(solubility)
at a constant temperature, the amount of a given gas that dissolves in a given type and volume of liquid is directly proportional to the partial pressure of that gas in equilibrium with that liquid
What is Boyle’s law?
(gas and volume)
at a constant temp, the volume of a gas is inversely proportional to the pressure of that gas
what is Charles’ law?
(volume and temperature)
at a contant pressure, the volume of a gas is proportional to the temperature of that gas
what is the average PO2 in the repertory airways?
13.5 kPa
what is the structure of haemoglobin monomers?
have a ferrous iron ion (Fe2+) at the centre of the tetrapyyrole porphyrin ring, connected to a protein chain (globin), covalently bonded at the proximal histamine residue
What are the 4 chains in normal haemoglobin (HbA)?
2 alpha and 2 beta chains
what are the 4 chains in HbA2?
it has 2 alpha and 2 delta chains
NOTE: HbA2 is a normal variant of haemoglobin
it constitutes around 2% of all haemoglobin
what are the 4 chains in foetal haemoglobin?
2 alpha and 2 gamma chains
present in trace levels
Haemoglobin is allosteric. What does this mean?
The binding of oxygen to one of the subunits is affected by its interactions with the other subunits.
The binding of oxygen to one haemoglobin subunit induces conformational changes that are relayed to the other subunits, making them more able to bind oxygen by raising their affinity for this molecule.
Thus the binding of oxygen to haemoglobin is said to be cooperative.
As oxygen binds, what happens to the centre of the tetramer?
a conformational change occurs that makes the centre a binding site for 2,3-DPG (a glycolytic by-product)
When ATP is being produced in large amounts, what happens to the levels of 2,3-DPG?
it increases
therefore, its levels are reflective of the levels of metabolism
What effect does 2,3-DPG when it binds to the centre of haemoglobin?
it decreases the affinity of haemoglobin for oxygen i.e. promotes the unloading of oxygen.
When metabolism is higher, more oxygen unloading is required, 2,3-DPG will bind and ‘squeeze’ out the oxygen so there is more available for the repairing tissue
What is haemoglobin co-operativity?
the haemoglobin changes shape and affinity based on how much oxygen is bound
what kind of relationship does dissolved oxygen have with PO2?
linear (but very shallow): the greater the partial pressure of oxygen, the more oxygen is dissolved
What kind of shape is the oxygen dissociation curve?
sigmoid - this gives effectively 100% saturation across a big range of alveolar PO2.
Under what circumstances would the ODC shift right? (Bohr shift)
(promotes unloading of oxygen)
(decreased affinity for oxygen)
NOTE: all of these take place when you EXERCISE /increase energy consumption:
- increased temperature
- acidosis (due to increase in lactic acid and excess CO2)
- hypercapnia (elevated CO2 because there is more cellular metabolism)
- increased in 2,3-DPG
Under what circumstances would the ODC shift left?
(promotes loading of oxygen) (increased affinity for oxygen) NOTE: opposite effects of exercise - decreased temperature - alkalosis - hypocapnia - decreased 2,3-DPG