Fetal haemoglobin has X affinity for oxygen than that of mothers haemo...
Fetal haemoglobin is the main oxygen transport carrier in human fetus during the last seven months of development in the uterus and persists in the newborn until it is about 6 months old. Functionally, fetal haemoglobin has a higher affinity to bind with oxygen molecules than the adult (or maternal) haemoglobin, giving the developing fetus better access to oxygen from the mother's blood stream.
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Fetal haemoglobin has X affinity for oxygen than that of mothers haemo...
Understanding Fetal Hemoglobin
Fetal hemoglobin (HbF) is essential for effective oxygen transport from the mother to the fetus during gestation. Its structure and affinity for oxygen differ from adult hemoglobin (HbA).
Higher Affinity for Oxygen
- HbF has a higher affinity for oxygen compared to maternal hemoglobin (HbA).
- This increased affinity allows the fetus to extract oxygen from maternal blood effectively, even in lower oxygen environments.
Why Higher Affinity?
- The structural differences between HbF and HbA contribute to this higher affinity.
- HbF contains two alpha and two gamma chains, while HbA consists of two alpha and two beta chains.
- The gamma chains in HbF reduce the binding of 2,3-bisphosphoglycerate (2,3-BPG), a molecule that decreases hemoglobin's affinity for oxygen. This reduction leads to a greater affinity for oxygen.
Physiological Significance
- The higher oxygen affinity of HbF is crucial for fetal development, ensuring adequate oxygen supply for growth and metabolism.
- As the fetus develops and approaches birth, HbF gradually transitions to HbA, which has a lower affinity for oxygen. This transition prepares the newborn for breathing air.
Conclusion
In summary, fetal hemoglobin has a higher affinity for oxygen than maternal hemoglobin throughout gestation. This property is vital for ensuring the fetus receives sufficient oxygen for development, highlighting the remarkable adaptation of human physiology during pregnancy.
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