4. Gas Transport and Exchange Flashcards
What do the following symbols stand for: • P • S • A • a
- P - partial pressure
- S - Hb saturation
- A - alveolar
- a - arterial
What does Dalton’s Law state?
Partial pressure of a [total] gas mixture is equal to the SUM of the partial pressure of [separate] gases in the mixture
What does Fick’s Law state?
Molecules diffuse from regions of high concentration to low concentration at a rate:
• proportional to the concentration gradient, exchange SA and diffusion capacity of the gas
• inversely proportional to the thickness of the gas exchange surface
What does Henry’s Law state?
• Constant temperature
• Amount of a given gas
- dissolves in a given type and volume of liquid
• Directly proportional to the partial pressure of that gas
- in equilibrium with that liquid
(bigger solubility coefficient - dissolves more easily)
What do Boyle’s and Charles’ Law both state?
Boyle’s Law
• Constant temperature
• Volume inversely proportional to pressure
Charles’ Law
• Constant pressure
• Volume directly proportional to temperature
What do you change if you are supplementing oxygen to someone with a diffusion problem?
Steepen the diffusion gradient
How do gases change at a greater altitude?
- Pressure decreases
- Smaller volume
- Proportions of gases remain the same
What is the PO2 of oxygen in dry air?
21.3 kPa
How does the PH2O change down the conducting airways?
Increases as dry air gets warmed, humidified, slowed and mixed with air already in the lungs
What is the PO2 at the respiratory airways?
- 13.5 kPa
* This is 100% saturation
Why can’t we rely on solely dissolved oxygen to keep us alive?
- 0.32mL/dL => 16mL/min
- Can only dissolve 17mL of oxygen
- Oxygen consumption (VO2) is around 250mL/min
Describe the structure of haemoglobin
- Monomer has Fe2+ (ferrous iron) at the centre of the tetrapyrrole porphyrin ring
- Connected to a protein chain (globin)
- Covalently bonded at the proximal histamine residue
- Tetramer with 2 alpha and 2 beta chains - HbA
- HbA2 - normal variant (2%) with 2 alpha and 2 delta chains
- Foetal (HbF) - trace levels, 2 alpha and 2 gamma chains
Describe the binding of oxygen to haemoglobin
- Haemoglobin has a low affinity for oxygen when not bound
- Oxygen binds - conformational changes (allosteric), greater affinity
- Each haem binds one molecule of oxygen
- Affinity for 4th oxygen is 300x that of the first oxygen
- Conformational change also occurs in the middle - becomes a binding site for 2,3-DPG (glycolytic by-product, reflective of metabolism)
- 2,3-DPG decreases the affinity of haemoglobin for oxygen
- Oxygen can be squeezed out where metabolism is high, so more is available for respiration in these places
What is cooperativity?
Describes how haemoglobin changes shape and affinity based on how much oxygen is bound
What is methaemoglobin?
- Fe2+ (ferrous iron) is oxidised to its ferric form (Fe3+) - becoming MetHb
- Doesn’t bind to oxygen
- Methaemoglobinaemia can cause functional anaemia (normal Hct but impaired O2 capacity)
What can oxidise Hb into MetHb, and what can be used to correct his?
- Nitrites - oxidise
* Methylene blue - correction