Human fetal haemoglobin differs from the adult haemoglobin in that it has
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because it's all depends upon the globin chain
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Fetal hemoglobin, or foetal haemoglobin, (also hemoglobin F, HbF, or α2γ2) is the main oxygen transport protein in the human fetus during the last seven months of development in the uterus and persists in the newborn until roughly 2-4 months old. Functionally, fetal hemoglobin differs most from adult hemoglobin in that it is able to bind oxygen with greater affinity than the adult form, giving the developing fetus better access to oxygen from the mother's bloodstream.
In newborns, fetal hemoglobin is nearly completely replaced by adult hemoglobin by approximately 6 months postnatally, except in a few thalassemia cases in which there may be a delay in cessation of HbF production until 3–5 years of age. In adults, fetal hemoglobin production can be reactivated pharmacologically,which is useful in the treatment of diseases such as sickle-cell disease.
In newborns, fetal hemoglobin is nearly completely replaced by adult hemoglobin by approximately 6 months postnatally, except in a few thalassemia cases in which there may be a delay in cessation of HbF production until 3–5 years of age. In adults, fetal hemoglobin production can be reactivated pharmacologically,which is useful in the treatment of diseases such as sickle-cell disease.
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