Chemistry
Chemistry
10th Edition
ISBN: 9781305957404
Author: Steven S. Zumdahl, Susan A. Zumdahl, Donald J. DeCoste
Publisher: Cengage Learning
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Q13:

**Educational Website Transcription: Hemoglobin and Myoglobin Binding Curves**

### Graph Explanation
The graph visualizes the binding curves of adult hemoglobin (in green) and myoglobin (in red) at pH 7.4, incorporating 2,3-bisphosphoglycerate. The hemoglobin binding curve is sigmoidal due to its four interacting oxygen-bound sites, while the myoglobin curve is hyperbolic, representing its single oxygen-bound site.

### Binding Curve Shifts
Determine whether the hemoglobin binding curve will shift left or right under the following scenarios:

#### Shifts Left

1. **Hemoglobin is isolated from red blood cells and stripped of 2,3-bisphosphoglycerate.**
2. **Tetrameric hemoglobin is dissociated into its subunits.**
3. **The adult hemoglobin (HbA) is replaced by an infant's fetal hemoglobin (HbF).**

#### Shifts Right

1. **The concentration of 2,3-bisphosphoglycerate increases during acclimation to high altitude.**
2. **The CO₂ concentration in the blood increases.**
3. **The blood pH drops from 7.4 to 7.2.**

### Graph Details
- **X-axis**: Partial pressure of oxygen (pO₂) in torr.
- **Y-axis**: Fraction of binding sites occupied.

The myoglobin curve remains relatively flat and quickly saturates as pO₂ increases, whereas the hemoglobin curve starts with a low fraction of occupied sites and increases sharply, indicating cooperative binding.
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Transcribed Image Text:**Educational Website Transcription: Hemoglobin and Myoglobin Binding Curves** ### Graph Explanation The graph visualizes the binding curves of adult hemoglobin (in green) and myoglobin (in red) at pH 7.4, incorporating 2,3-bisphosphoglycerate. The hemoglobin binding curve is sigmoidal due to its four interacting oxygen-bound sites, while the myoglobin curve is hyperbolic, representing its single oxygen-bound site. ### Binding Curve Shifts Determine whether the hemoglobin binding curve will shift left or right under the following scenarios: #### Shifts Left 1. **Hemoglobin is isolated from red blood cells and stripped of 2,3-bisphosphoglycerate.** 2. **Tetrameric hemoglobin is dissociated into its subunits.** 3. **The adult hemoglobin (HbA) is replaced by an infant's fetal hemoglobin (HbF).** #### Shifts Right 1. **The concentration of 2,3-bisphosphoglycerate increases during acclimation to high altitude.** 2. **The CO₂ concentration in the blood increases.** 3. **The blood pH drops from 7.4 to 7.2.** ### Graph Details - **X-axis**: Partial pressure of oxygen (pO₂) in torr. - **Y-axis**: Fraction of binding sites occupied. The myoglobin curve remains relatively flat and quickly saturates as pO₂ increases, whereas the hemoglobin curve starts with a low fraction of occupied sites and increases sharply, indicating cooperative binding.
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