Campbell Biology in Focus
3rd Edition
ISBN: 9780134710679
Author: Lisa A. Urry, Michael L. Cain, Steven A. Wasserman, Peter V. Minorsky, Rebecca Orr
Publisher: PEARSON
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Chapter 34, Problem 11TYU
Summary Introduction
To relate:
The mechanism of O2 transport in the human body with the preparation of athletes to climb mountains.
Introduction:
The oxygen content in the atmosphere is 21%. As a person goes up the altitude, the partial pressure of oxygen (
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Andrew has lived his whole life in San Diego, CA at sea level. One summer in college he gets a job as a field biologist in the Colorado Rockies (elevation
7500 ft. above sea level). The first week he is in Colorado he experiences altitude sickness from the change in atmosphere. Altitude sickness is
characterized by fatigue and shortness of breath as a result of the thinner air which contains less oxygen.
a. How does Andrew's fatigue and shortness of breath relate to the cellular respiration pathway?
be.
b. What would you expect to find if you test the level of lactic acid in Andrew's blood? Explain your answer.
.9
C. A couple weeks later, Andrew is feeling better but he noticed that his appetite has increased. Explain why this might be.
Provide an example of HOW the body over time can improve each
How will O2 transportation increase?
How would the body increase internal respiration?
How could the body increase energy production via cellular respiration?
A crocodile, which can remain underwater without breathing for up to 1 hour drowns its air-breathing prey, then dines at its leisure. An adaptation that aids the crocodile in doing so is that it can utilize virtually 100% of the O2 in its blood whereas humans, for example, can only extract about 65% of the O2 in their blood. Crocodile Hb does not bind BPG. However, crocodile deoxyHb preferentially binds HCO3-. How does this help the crocodile obtain its dinner?
Please help explain why/if this is the answer, thank you!
As CO2 concentrations increase so will the concentration of HCO3-. The HCO3- preferentially binds to the crocodile's deoxyhemoglobin, which allosterically prompts the hemoglobin to assume the deoxy conformation and thus release its O2.
Chapter 34 Solutions
Campbell Biology in Focus
Ch. 34.1 - How is the now of hemolymph through an open...Ch. 34.1 - Three-chambered hearts with incomplete septa were...Ch. 34.1 - Prob. 3CCCh. 34.2 - Prob. 1CCCh. 34.2 - Why is it important that the AV node delay the...Ch. 34.2 - Prob. 3CCCh. 34.3 - What is the primary cause of the low velocity of...Ch. 34.3 - Prob. 2CCCh. 34.3 - Prob. 3CCCh. 34.4 - Prob. 1CC
Ch. 34.4 - Prob. 2CCCh. 34.4 - Prob. 3CCCh. 34.4 - Prob. 4CCCh. 34.5 - Why is an internal location for gas exchange...Ch. 34.5 - After a heavy rain, earthworms come to the...Ch. 34.5 - MAKE CONNECTIONS Describe similarities in the...Ch. 34.6 - Prob. 1CCCh. 34.6 - Prob. 2CCCh. 34.6 - WHAT IF? If an injury tore a small hole in the...Ch. 34.7 - What determines whether O2, or CO2, undergoes net...Ch. 34.7 - How does the Bohr shift help deliver O2, to very...Ch. 34.7 - Prob. 3CCCh. 34 - Which of the following respiratory systems is not...Ch. 34 - Blood returning to the mammalian heart in a...Ch. 34 - Pulse is a direct measure of A. blood pressure. B....Ch. 34 - Prob. 4TYUCh. 34 - One feature that amphibians and humans have in...Ch. 34 - If a molecule of CO2 released into the blood in...Ch. 34 - Prob. 7TYUCh. 34 - DRAW IT Plot blood pressure against time for one...Ch. 34 - Prob. 9TYUCh. 34 - Prob. 10TYUCh. 34 - Prob. 11TYUCh. 34 - SYNTHESIZE YOUR KNOWLEDGE The diving bell spider...
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- multiple choicearrow_forwardPart 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…arrow_forwardIf there were little to no Chloride in the blood, what would happen to CO2 transport and why? Select one: O a. CO2 transport would not change because chloride is not part of the carbonic anhydrase reaction O b. CO2 transport would decline because H+ would not be able to bind to hemoglobin O c. CO2 transport would decline because HCO3 wouldn't be able to exit the red blood cell thus inhibiting the carbonic anhydrase reaction O d. CO2 transport would increase because HCO3 would be able to exit the red blood cell more freelyarrow_forward
- Please answer correctly and fastarrow_forwardAll our body tissues require O2 for their function. And, Hemoglobin does this job, i.e., hemoglobin transport the O2 to all the tissues. How will these conditions affect O2 transportation? i. If CO2 increases in the lung.ii. If pH increases in the stomach tissue.arrow_forwardChoose all the correct answers for oxygen carrying proteinsarrow_forward
- 18arrow_forward. Carbonic anhydrase of erythrocytes (M, 30,000) has one of the highest turnover numbers known. It catalyzes the reversible hydration of CO₂. H₂O + CO₂ H₂CO3 This is an important process in the transport of CO₂ from the tissues to the lungs. If 3 µg of pure carbonic anhydrase catalyzes the hydration of 0.10 g of CO₂ in 1 min at 37 °C at Vmax, what is the turnover number (kcat) of carbonic anhydrase? Keat = 3.79 ×10-¹4 Incorrect I minarrow_forwardWhat statement about hemoglobin's integrated transport of oxygen, carbon dioxide and protons is FALSE? Question 26 options: Lower pH leads to more oxygen being released into the tissues Protons can bind hemoglobin at a variety of sites, including histidine side chains. Proton binding stabilizes the R-form of hemoglobin. Hemoglobin binds bicarbonate and transports it from the tissues to the lungs Carbon dioxide binds to hemoglobin in the tissues and gets transported back to the lungsarrow_forward
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