Question 1. What is the O₂ saturation in the lungs? 2. What is the O₂ saturation in tissues at rest? 3. What percentage of O₂ is delivered to tissues at rest? 4. What is the O₂ saturation in exercising tissues? 5. What percentage of O₂ is delivered to exercising tissues? Cooperative binding Noncooperative binding

Biochemistry
9th Edition
ISBN:9781319114671
Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.
Publisher:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.
Chapter1: Biochemistry: An Evolving Science
Section: Chapter Questions
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The table below walks you through a comparison of cooperative binding and noncooperative binding. By completing the table, you will learn why cooperative binding
is an important adaptation that makes gas exchange more efficient.
Drag the labels to their appropriate locations on the table. Labels can be used more than once.
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50%
70%
80%
100%
Question
1. What is the O₂2 saturation
in the lungs?
2. What is the O₂ saturation
in tissues at rest?
3. What percentage of O₂ is
delivered to tissues at rest?
4. What is the O₂ saturation
in exercising tissues?
5. What percentage of O₂ is
delivered to exercising tissues?
Cooperative binding
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Noncooperative binding
Transcribed Image Text:The table below walks you through a comparison of cooperative binding and noncooperative binding. By completing the table, you will learn why cooperative binding is an important adaptation that makes gas exchange more efficient. Drag the labels to their appropriate locations on the table. Labels can be used more than once. ► View Available Hint(s) 20% 30% 50% 70% 80% 100% Question 1. What is the O₂2 saturation in the lungs? 2. What is the O₂ saturation in tissues at rest? 3. What percentage of O₂ is delivered to tissues at rest? 4. What is the O₂ saturation in exercising tissues? 5. What percentage of O₂ is delivered to exercising tissues? Cooperative binding Reset Help Noncooperative binding
Part C - Exploring the cooperative binding of oxygen
Oxygen shows cooperative binding to hemoglobin. Cooperative binding has the following effects on the binding and release of oxygen:
Oxygen binding to hemoglobin: When one molecule of oxygen binds to one of hemoglobin's four subunits, the other subunits change shape slightly, increasing
their affinity for oxygen.
Oxygen release from hemoglobin: When four oxygen molecules are bound to hemoglobin's subunits and one subunit releases its oxygen, the other three subunits
change shape again. This causes them to release their oxygen more readily.
These two graphs show how cooperative binding differs from a hypothetical situation where binding is not cooperative.
• The x-axis shows the partial pressure of oxygen (PO₂). This is a measure of the amount of oxygen present in a tissue. The blue arrows on the x-axis
show the partial pressure of oxygen in various tissues of the body.
• The y-axis shows the oxygen saturation of hemoglobin (O₂ saturation). This is the percentage of oxygen-binding sites on hemoglobin molecules
that are actually bound to oxygen.
O₂ saturation of hemoglobin (%)
100
80
60
40-
20
0
0
Cooperative binding
10 20 30 40 50 60 70
tissue during
exercise
tissue
at rest
PO₂ (mm Hg)
80 90 100
lungs
O₂ saturation of hemoglobin (%)
100
80
60
40
20
0
0
Noncooperative binding
10 20 30
tissue during
exercise
40
50 60 70 80
tissue
at rest
PO2 (mm Hg)
90 100
lungs
Adapted from Biological Science by Freeman Ⓒ Pearson Education, Inc.
The table below walks you through a comparison of cooperative binding and noncooperative binding. By completing the table, you will learn why cooperative binding
is an important adaptation that makes gas exchange more efficient.
Drag the labels to their appropriate locations on the table. Labels can be used more than once.
Transcribed Image Text:Part C - Exploring the cooperative binding of oxygen Oxygen shows cooperative binding to hemoglobin. Cooperative binding has the following effects on the binding and release of oxygen: Oxygen binding to hemoglobin: When one molecule of oxygen binds to one of hemoglobin's four subunits, the other subunits change shape slightly, increasing their affinity for oxygen. Oxygen release from hemoglobin: When four oxygen molecules are bound to hemoglobin's subunits and one subunit releases its oxygen, the other three subunits change shape again. This causes them to release their oxygen more readily. These two graphs show how cooperative binding differs from a hypothetical situation where binding is not cooperative. • The x-axis shows the partial pressure of oxygen (PO₂). This is a measure of the amount of oxygen present in a tissue. The blue arrows on the x-axis show the partial pressure of oxygen in various tissues of the body. • The y-axis shows the oxygen saturation of hemoglobin (O₂ saturation). This is the percentage of oxygen-binding sites on hemoglobin molecules that are actually bound to oxygen. O₂ saturation of hemoglobin (%) 100 80 60 40- 20 0 0 Cooperative binding 10 20 30 40 50 60 70 tissue during exercise tissue at rest PO₂ (mm Hg) 80 90 100 lungs O₂ saturation of hemoglobin (%) 100 80 60 40 20 0 0 Noncooperative binding 10 20 30 tissue during exercise 40 50 60 70 80 tissue at rest PO2 (mm Hg) 90 100 lungs Adapted from Biological Science by Freeman Ⓒ Pearson Education, Inc. The table below walks you through a comparison of cooperative binding and noncooperative binding. By completing the table, you will learn why cooperative binding is an important adaptation that makes gas exchange more efficient. Drag the labels to their appropriate locations on the table. Labels can be used more than once.
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