why hbf has high affinity for oxygen?
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Affinity of HbF for oxygen. The high affinity of HbF for O2 favors the taking up of oxygen in the placenta. This high affinity of HbF for O2 is explained by its low affinity for 2,3 DPG (diphosphoglycerate), an organic phosphate present in the erythrocytes that normally competes with O2 for the binding to Hb.
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Human blood is red because of the protein hemoglobin, which contains a red-colored compound called heme that's crucial for carrying oxygen through your bloodstream. Heme contains an iron atom which binds to oxygen; it's this molecule that transports oxygen from your lungs to other parts of the body.
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Hemoglobin is the protein that makes blood red. ... Oxygen binds reversibly to these iron atoms and is transported through blood. Each of the protein chains is similar in structure to myoglobin, the protein used to store oxygen in muscles and other tissues.
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These data suggest that the high HbF levels in HbE/β thalassemia, and other β thalassemia syndromes, result from increased erythropoietin levels leading to bone marrow expansion, and possibly increased F-cell production, combined with ineffective erythropoiesis giving a survival advantage to F cells.
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Pure oxygen can be deadly. Our blood has evolved to capture the oxygen we breathe in and bind it safely to the transport molecule called haemoglobin. If you breathe air with a much higher than normal O2 concentration, the oxygen in the lungs overwhelms the blood's ability to carry it away.
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This leftward shift indicates that the hemoglobin under study has an increased affinity for oxygen so that hemoglobin binds oxygen more easily, but unloads it more reluctantly. Left shift of the curve is a sign of hemoglobin's increased affinity for oxygen (e.g. at the lungs).
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Each iron ion in the heme can bind to one oxygen molecule; therefore, each hemoglobin molecule can transport four oxygen molecules. An individual erythrocyte may contain about 300 million hemoglobin molecules, and therefore can bind to and transport up to 1.2 billion oxygen molecules (see Figure 3b).
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 Red blood cells are able to carry oxygen so efficiently because of a special protein inside them: haemoglobin.   In fact, it is the haemoglobin that is responsible for the colour of the red blood cell.   Haemoglobin contains a haem prosthetic group that has an iron atom at its centre.
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Fetal hemoglobin (HbF) modulates the phenotype of sickle cell anemia by inhibiting deoxy sickle hemoglobin (HbS) polymerization. The blood concentration of HbF, or the number of cells with detectable HbF (F-cells), does not measure the amount of HbF/F-cell.
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Hemoglobin in blood carries oxygen from the lungs or gills to the rest of the body (i.e. the tissues). There it releases the oxygen to permit aerobic respiration to provide energy to power the functions of the organism in the process called metabolism.
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The Haldane effect describes how oxygen concentrations determine hemoglobin's affinity for carbon dioxide. For example, high oxygen concentrations enhance the unloading of carbon dioxide. ... The Bohr effect, on the other hand, describes how carbon dioxide and H+ affect the affinity of hemoglobin for oxygen.
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Hemoglobin is basically an Oxygen carrying compound. Carrying it inside red blood cells enables it to compartmentalize oxygen delivery, and be able to release it to tissues under the right conditions. Being inside the RBC ensures that the pH and ionic milleu is optimum for this function.
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- The right shift shows a decrease in affinity. Hemoglobin is more likely to release Oxygen. This is due to high temperature, high metabolism, and low pH. While Hemoglobin has 4 subunits, Myoglobin has one subunit.
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Haemoglobin is found in red blood cells and carries oxygen efficiently from the lungs to the tissues in body. It also aids in transporting hydrogen ions and carbon dioxide back to the lungs. ... Haemoglobin is composed of four subunits each containing a cofactor known as a haem group that includes an iron atom center.
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A hemoglobin test measures the levels of hemoglobin in your blood. Hemoglobin is a protein in your red blood cells that carries oxygen from your lungs to the rest of your body. If your hemoglobin levels are abnormal, it may be a sign that you have a blood disorder. Other names: Hb, Hgb.
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Each molecule of haemoglobin can hold four oxygen molecules. It is haemoglobin that carries the oxygen as it is transported around the body in the blood. Only a small amount of oxygen (1.5% in arterial blood) is simply dissolved in the plasma. Haemoglobin is the main component in oxygen transport throughout the body.
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In the blood, oxygen is bonded to molecules of hemoglobin in red blood cells for transport.