Rapidly metabolizing tissues generate large amounts of protons and carbon dioxide. The result of this increase in protons and carbon dioxide is the oxygen-binding curve of hemoglobin O changes shape from sigmoidal to hyperbolic. O shifts to the left, meaning more binding of O2 at lower O2 levels. O remains the same. O shifts to the right, meaning lower saturation at higher O2 levels.
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The question describes a scenario where rapidly metabolizing tissues produce large amounts of protons (H+) and carbon dioxide (CO2). It then asks about the effect of this increase on the oxygen-binding curve of hemoglobin. Show more…
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The graph represents the adult hemoglobin binding curve (in green) at pH 7.4 in the presence of 2,3-bisphosphoglycerate. The hemoglobin binding curve has a sigmoidal shape, due to four interacting oxygen-bound sites. For comparison, the myoglobin binding curve has only one oxygen-bound site and has a hyperbolic curve. For each of the six scenarios, determine whether the hemoglobin binding curve would shift left or shift right. Shifts left Shifts right Answer Bank Tetrameric hemoglobin is dissociated into its subunits. The concentration of 2,3-bisphosphoglycerate increases during acclimation to high altitude. The adult hemoglobin (HbA) is replaced by an infant's fetal hemoglobin (HbF). The CO2 concentration in the blood increases. The blood pH drops from 7.4 to 7.2. Hemoglobin is isolated from red blood cells and stripped of 2,3-bisphosphoglycerate.
Adi S.
Higher Hb-O2 affinity (left shift) lower CO2 higher pH lower temperature Reduced Hb-O2 affinity (right shift) higher CO2 lower pH higher temperature PO2 (mm Hg) The dissociation and binding of oxygen to Hgb are not directly proportional; instead they exhibit a sigmoid curve known as the hemoglobin-oxygen dissociation curve. The curve is important because it shows how a large amount of oxygen can be delivered to the tissues with a small drop in oxygen saturation.
The graph represents the adult hemoglobin binding curve (in green) at pH 7.4 in the presence of 2,3-bisphosphoglycerate. The hemoglobin binding curve has a sigmoidal shape, due to four interacting oxygen-bound sites. For comparison, the myoglobin binding curve has only one oxygen-bound site and has a hyperbolic curve. For each of the six scenarios, determine whether the hemoglobin binding curve would shift left or shift right. Myoglobin Hemoglobin pO2 (torr) Shifts left Shifts right
Imaan A.
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