· Intro
· Interaction with haemoglobin
· Clinical applications
Nature |
· Three carbon metabolic intermediate · Highly negatively charged · High concentration in RBC |
Pathway |
|
Increased if |
· High altitude · Chronic lung disease · Anaemia |
Adult Hb |
· Binds to the β-globin chain · Stabilises the tense (T) low affinity conformation · Hence right shift of oxyhaemoglobin dissociation curve (OHDC) -> ↑p50 · Aids O2 unloading at tissue capillaries · Reverse at the lungs -> O2 loading · Effect on gas exchange vivo appears less significant than predicted
|
Foetal Hb |
· Serine instead of histidine at position 143 on globin chain · Histidine positively charged, interacts with negative charges on 2,3-DPG · Serine neutrally charged, does not interact · Hence very low affinity for 2,3-DPG · Left shift of OHDC, lower p50 (19mmHg cf. 26mmHg) |
Altitude |
· ↑2,3-DPG production due to ↓PaO2 · Right shift OHDC -> ↓O2 affinity -> ↑tissue oxygenation -> ↑EO2 · Only partly offsets L shift caused by resp alkalosis (↓PaCO2, ↑pH) |
Anaemia |
· ↑2,3-DPG production due to ? cellular hypoxia · ↓Affinity -> ↑tissue oxygenation -> ↑EO2 |
Stored RBC |
· 50% ↓[2,3-DPG] at 2/52 · 95% ↓ at 4/52 · Due to ↓temp -> ↓glycolysis and lack of substrate · Left shift OHDC -> ↑O2 affinity -> ↓EO2 -> tissue oxygenation · [2,3-DPG] restored after 24 hours |
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