Respiratory expert session - 06.11.17 Flashcards
What are the normal PaO2, PaCO2, pH and HCO3- values?
PaO2: 10 - 13.5 kPa
PaCO2: 4.8 - 6 kPa
pH: 7.35 - 7.45
HCO3-: 23 - 27mmol/L
What is the alveolar gas equation?
PAO2 = FiO2(Patm - PH2O) - PaCO2/RER
FiO2 - 0.21 Patm - 101kPa PH2O - 6.25kPa PaCO2 - from blood analysis RER - 0.8
What is the alveolar-arterial difference and what is the normal range?
is a measure of the difference between alveolar and arterial oxygen
- 0.5-1.5kPa
What type of protein is Hb?
Allosteric protein
What is meant by “cooperative binding”?
Binding of oxygen to one haemoglobin subunit causes a conformational change that are relayed to the other subunits, making them more able to bind oxygen by raising their affinity for this molecule - oxygen binding to iron is reversible and changes the structure of the subunit - the new conformation causes the haem groups to become progressively more exposed
What is the key purpose of Hb?
increases the total blood oxygen capacity seventy fold in comparison to dissolved oxygen in the blood
What form is oxygenated Hb?
has a planar form = referred to as R or relaxed form
What does the Bohr effect?
facilitates oxygen release in the tissues
What effect does the Bohr effect have on the oxygen-dissociate?
Shifts to the right
because this decreases the pH of the blood which promotes the dissociation of oxygen
When does Hb have a higher binding affinity for H+?
Hb has proton binding sites which have a higher affinity for binding H+ in deoxyhaemoglobin than oxyhaemoglobin
- oxygen is pushed off Hb to accommodate proton binding
What conc is 2,3-BPG present in the blood?
approx. 5mmol/L
Which form of Hb does 2,3-BPG bind to with a greater affinity?
Binds with a greater affinity to deoxygenated Hb (e.g. RBCs near respiring tissue) than it does to oxygenated Hb (e.g. lungs) due to spatial changes
- 2,3-BPG fits in the non-planar de-oxygenated Hb configuration but not in the oxygenated planar formation
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What part of Hb does 2,3-BPG interact with?
interacts with deoxygenated Hb beta subunits decreasing O2 affinity so it allosterically promotes the release of the remaining oxygen molecules bound to Hb
What are “salt bridges”?
in the presence of CO2 and H+, charged groups are formed on each subunit - charged groups form salt bridges
These form between 2 subunits and stabilise the deoxygenated form of Hb
What light does oxygenated conformation of Hb absorb and reflect?
light in the blue-green range and reflects red light, giving the red appearance of oxygenated blood