(a)
To determine: Whether HbA or HbF hemoglobin has a higher affinity for oxygen under physiological conditions.
Introduction:
Hemoglobin is the blood protein that carries the oxygen molecule. It is composed of four heme groups which surround the globin group. Heme groups possess iron and provides a red color to the blood cells. Hemoglobin is present in the tetrameric form that consist 2 dimers (α,ß dimmers) that binds to the oxygen molecule. The affinity of oxygen to bind with hemoglobin is isolated from the red blood cells that displays a sigmoidal curve. 2,3- bisphosphoglycerate is a glycolytic intermediate that has an immense affinity for the deoxyhemoglobin molecule.
(b)
To determine: The physiological significance of the different O2 affinities.
Introduction:
Hemoglobin is the blood protein that carries the oxygen molecule. It is composed of four heme groups which surround the globin group. Heme groups possess iron and provides a red color to the blood cells. Hemoglobin is present in the tetrameric form that consist 2 dimers (α, ß dimmers) that binds to the oxygen molecule. The affinity of oxygen to bind with hemoglobin is isolated from the red blood cells that displays a sigmoidal curve. 2,3- bisphosphoglycerate is a glycolytic intermediate that has an immense affinity for the deoxyhemoglobin molecule.
(c)
To determine: The effect of BPG on the oxygen affinity of hemoglobin and explain the different oxygen affinities of fetal and maternal hemoglobin.
Introduction:
Hemoglobin is the blood protein that carries the oxygen molecule. It is composed of four heme groups which surround the globin group. Heme groups possess iron and provides a red color to the blood cells. Hemoglobin is present in the tetrameric form that consist 2 dimers (α,ß dimmers) that binds to the oxygen molecule. The affinity of oxygen to bind with hemoglobin is isolated from the red blood cells that displays a sigmoidal curve. 2,3- bisphosphoglycerate is a glycolytic intermediate that has an immense affinity for the deoxyhemoglobin molecule.
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