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.