Respiratory - Oxygen Transport Flashcards
What is Huffner’s constant?
It is the measured maximum oxygen carrying capacity of haemoglobin.
1.34 ml O2 / gram Hb
How is O2 transported in blood - give proportions
Bound to Hb - 98%
Dissolved in plasma - 2%
What is the Oxygen content equation
CaO2 = {1.34 x [Hb] x SaO2/100%} +0.023 x PO2
This equation gives ml of O2 per 100 ml of blood
CaO2 = 19.8 ml O2 per 100 ml blood CvO2 = 15.2 ml O2 per 100 ml blood
What is Henry’s law in the context of O2 transport
The volume of O2 dissolved in blood is proportional to the partial pressure of O2
Why is dissolved O2 important despite being such small percentage of O2 in transit. Quote Fick’s law in the explanation
The PaO2 is determined from the amount of O2 dissolved in plasma - PO2 within RBC is small as O2 is bound to Hb.
Fick’s law of diffusion states diffusion occurs along a pressure gradient - so O2 diffuses into the tissues from the dissolved portion in the plasma, not from Hb itself. O2 dissociates from Hb to replenish the plasma O2.
How do the body’s O2 stores compare with its consumption of O2
70 kg adult STORES: 1. Blood - 850 ml O2 2. Myoglobin - 250 ml O2 3. Lungs - 450 ml O2
Total 1550 ml
CONSUMPTION
1. 250 ml/min at rest
1550 ml O2 divided by 250 ml/minute
= ± 6 minutes
O2 consumption increased in kids
Reduced O2 carrying capacity –>anaemia / CO poisoning
Describe the structure of red blood cells
Small, flexible, biconcave discs of diameter 6 - 8 micrometers that are able to deform enough to squeeze through the smallest capillaries around 3 micrometers in diameter.
Cell membrane has NB Ag’s NB in blood transfusion medicine: ABO (cell surface CHO based Ags) and Rhesus (Transmembrane proteins)
Why are red blood cells unique cells
- No nucleus
- No mitochondria therefore anaerobic metabolism –> depend entirely on glucose and the glycolytic pathway
‘bags of Hb’
Nucleus is lost in the latter stages of maturation in the bone marrow during erythropoiesis (reticulocytes)
What percentage of circulating RBC’s are reticulocytes?
1% normally –> may increase if the bone marrow is highly active e.g. haemorrhage or haemolytic anaemia
Describe the structure of HbA
Quaternary structure (Tetrahedral)
- 4 polypeptide globin subunits (2 alpha and 2 beta chains)
- Globin chains held together by weak electrostatic forces
- Each globin chain has:
1. Haem group (iron containing porphyrin ring with iron in the Ferrous state Fe2+)
2. O2 molecules are bound to each haem group
How many O2 molecules can bind to one Hb molecule
Four - One bound to each haem group (Fe2+ ion)
What is co-operative binding
Increase in O2 affinity of Hb with each successive O2 binding
The last of 4 O2 molecules to bind binds 300 times more easily than the first
This results in the sigmoid shaped curve of the OHDC and when four O2 molecules are bound the Hb is in the ‘relaxed’ as opposed to the tense conformation
What is the OHDC and why is its sigmoid shape clinically relevant?
OHDC describes the relationship between SaO2 and blood O2 tension.
Distal - plateau portion curve large changes in PaO2 with minimal change to SaO2.
Initial steep part of the curve - small changes in PaO2 –> large changes in SaO2.
Describe the causes of left and right shift of the P50 on the OHDC
RIGHT SHIFT
High H+ (acidosis) High CO2 High temperature 2,3 DPG HbS Exercise
LEFT SHIFT
Low H+ (Alkalosis) Low CO2 Low temperature Low 2,3, DPG MetHb COHb HbF
What is the Bohr effect
Metabolically active tissues produce CO2, H ions and heat –. blood arrives at capillaries and is exposed to this –> OHDC shifts right –> offloading O2 where it is most needed
