The The graph represents the adult hemoglobin binding curve (in green) at pH 7.4 in the presence of 2,3-bisphosphoglycerate. hemoglobin binding curve has a sigmoidal shape, due to four interacting oxygen-bound sites. For comparison, the myglobin 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 Answer Bank Hemoglobin is isolated from red blood cells and stripped of 2,3-bisphosphoglycerate. Tetrameric hemoglobin is dissociated into its subunits. The concentration of 2,3-bisphosphoglycerate increases during acclimation to high altitude. Fraction of binding sites occupied The adult hemoglobin (HbA) is replaced by an infant's fetal hemoglobin (HbF). 0.9 0.8 0.7 0.6 0.5 0.4 0.3 0.2 0.1 0.0 0 20 Myoglobin 40 The CO₂ concentration in the blood increases. Hemoglobin 60 po₂ (torr) Shifts right 80 The blood pH drops from 7.4 to 7.2. 100 12

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Chapter1: Chemical Foundations
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Q13:

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 myglobin
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
Answer Bank
Hemoglobin is isolated from red blood cells and stripped of 2,3-bisphosphoglycerate.
Tetrameric hemoglobin is dissociated into its subunits.
The concentration of 2,3-bisphosphoglycerate increases during acclimation to high altitude.
Fraction of binding sites occupied
The adult hemoglobin (HbA) is replaced by an infant's fetal hemoglobin (HbF).
0.8 H
0.7 H
0.6
0.5
0.4
0.3
0.2
0.1
0.0
L
20
Myoglobin
↓
40
The CO₂ concentration in the blood increases.
Hemoglobin
↓
60
pO₂ (torr)
Shifts right
80
The blood pH drops from 7.4 to 7.2.
100
120
Transcribed Image Text: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 myglobin 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 Answer Bank Hemoglobin is isolated from red blood cells and stripped of 2,3-bisphosphoglycerate. Tetrameric hemoglobin is dissociated into its subunits. The concentration of 2,3-bisphosphoglycerate increases during acclimation to high altitude. Fraction of binding sites occupied The adult hemoglobin (HbA) is replaced by an infant's fetal hemoglobin (HbF). 0.8 H 0.7 H 0.6 0.5 0.4 0.3 0.2 0.1 0.0 L 20 Myoglobin ↓ 40 The CO₂ concentration in the blood increases. Hemoglobin ↓ 60 pO₂ (torr) Shifts right 80 The blood pH drops from 7.4 to 7.2. 100 120
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