Fetal hemoglobin comprises of αγ sub-units. It has been found that the γ-chain contains serine at position 143 instead of Histidine 143 normally found in the β-chain. The amino acid 143 lines the DPG binding site. This mutation in the γ chain results in a) Increased Oxygen binding in the fetus. b) Increased efficiency of oxygen transport to the lungs in the fetus. c) Increased DPG binding in the fetal hemoglobin d) This is a silent mutation, i.e. no change should be observed.
Fetal hemoglobin comprises of αγ sub-units. It has been found that the γ-chain contains serine at position 143 instead of Histidine 143 normally found in the β-chain. The amino acid 143 lines the DPG binding site. This mutation in the γ chain results in a) Increased Oxygen binding in the fetus. b) Increased efficiency of oxygen transport to the lungs in the fetus. c) Increased DPG binding in the fetal hemoglobin d) This is a silent mutation, i.e. no change should be observed.
Human Anatomy & Physiology (11th Edition)
11th Edition
ISBN:9780134580999
Author:Elaine N. Marieb, Katja N. Hoehn
Publisher:Elaine N. Marieb, Katja N. Hoehn
Chapter1: The Human Body: An Orientation
Section: Chapter Questions
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Fetal hemoglobin comprises of αγ sub-units. It has been found that the γ-chain contains serine at position 143 instead of Histidine 143 normally found in the β-chain. The amino acid 143 lines the DPG binding site. This mutation in the γ chain results in
a) Increased Oxygen binding in the fetus.
b) Increased efficiency of oxygen transport to the lungs in the fetus.
c) Increased DPG binding in the fetal hemoglobin
d) This is a silent mutation, i.e. no change should be observed.
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