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OBG · Normal pregnancy and antenatal care: fetal haemoglobin
Sample itemFetal blood takes up oxygen from maternal blood across the placenta even though the fetal PaO2 is only about 30 mmHg. Which property of fetal haemoglobin (HbF) mainly explains this?
Original practice item, not a recalled exam question. Nothing here is recorded.
The answer and the reasoning
C. Poor 2,3-bisphosphoglycerate binding, giving higher oxygen affinity
HbF (alpha2 gamma2) binds 2,3-BPG poorly, so its oxygen dissociation curve lies to the left of that of HbA. Fetal blood therefore loads oxygen at the low PO2 found in the intervillous space. Fetal haemoglobin concentration is in fact higher than maternal, which further aids transfer.
Option by option
A. Strong 2,3-bisphosphoglycerate binding, giving higher oxygen affinity
Strong 2,3-BPG binding lowers oxygen affinity, as in adult HbA, and would hinder uptake.
B. A lower haemoglobin concentration than the maternal blood has
Fetal haemoglobin concentration is higher, not lower, than maternal, and this is not the mechanism.
C. Poor 2,3-bisphosphoglycerate binding, giving higher oxygen affinity (correct)
Correct. Weak 2,3-BPG binding by HbF shifts its curve left, so it saturates at lower PO2.
D. A rightward shift of the dissociation curve, favouring oxygen release
A rightward shift would reduce affinity and favour oxygen release to tissue, not uptake from the mother.
Source note: Original NextPrep sample item — pending expert review. This item is original practice material awaiting independent expert review, so confirm important facts in a standard textbook.
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