Principles of Anatomy and Physiology
16th Edition
ISBN: 9781119662792
Author: Tortora, Gerard J., DERRICKSON, Bryan H.
Publisher: WILEY
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Chapter 23, Problem 27CP
Summary Introduction
To review:
The unloading of oxygen in hemoglobin is more as the blood moves via the capillaries of the active tissues like skeletal muscle during exercise as compared to rest.
Introduction:
Partial pressure is the vital factor, which is considered to determine the percent of oxygen saturation of the hemoglobin. When completely reduced hemoglobin converts into oxyhaemoglobin, it is known to be saturated completely.
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After spending a day or more at high altitude (with an oxygen partial pressure of 75 torr), the concentration of 2,3- bisphosphoglycerate (2,3-BPG) in red blood cells increases. What effect would an increased concentration of 2,3-BPG have on the oxygen-binding curve for hemoglobin? Why would this adaptation be beneficial for functioning well at high altitude?
When oxygenated blood (Hemoglobin nearly 100% saturated), reaches resting systemic tissues, what percentage of the available oxygen is unloaded from hemoglobin? 100%, 75%, 50%, or 25%?
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Chapter 23 Solutions
Principles of Anatomy and Physiology
Ch. 23 - What are the three basic steps involved in...Ch. 23 - What are the components of the respiratory system?Ch. 23 - Why is the respiratory zone important?Ch. 23 - 4. Compare the structure and functions of the...Ch. 23 - 5. What are the functions of the three...Ch. 23 - Prob. 6CPCh. 23 - Prob. 7CPCh. 23 - 8. Describe the structure of the bronchial tree.
Ch. 23 - Prob. 9CPCh. 23 - Prob. 10CP
Ch. 23 - Prob. 11CPCh. 23 - Prob. 12CPCh. 23 - Prob. 13CPCh. 23 - Prob. 14CPCh. 23 - Describe how alveolar surface tension, compliance,...Ch. 23 - Demonstrate the various types of modified...Ch. 23 - Prob. 17CPCh. 23 - What is the difference between a lung volume and a...Ch. 23 - How is minute ventilation calculated?Ch. 23 - Prob. 20CPCh. 23 - Prob. 21CPCh. 23 - How does the partial pressure of oxygen change as...Ch. 23 - What are the diffusion paths of oxygen and carbon...Ch. 23 - 24. What factors affect the rate of diffusion of...Ch. 23 - Prob. 25CPCh. 23 - What is the relationship between hemoglobin and P...Ch. 23 - Prob. 27CPCh. 23 - Prob. 28CPCh. 23 - How is the pontine respiratory group related to...Ch. 23 - Prob. 30CPCh. 23 - How does exercise affect the DRG?Ch. 23 - What structures develop from the laryngotracheal...Ch. 23 - What accounts for the decrease in lung capacity...Ch. 23 - Aretha loves to sing. Right now she has a cold, a...Ch. 23 - Ms. Brown has smoked cigarettes for years and is...Ch. 23 - The Robinson family went to bed one frigid winter...
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- How does hemoglobin help maintain the oxygen partial pressure gradient during gas transport in the body?arrow_forwardWhat is oxyhemoglobin? Where does it form?arrow_forwardIn the text, we learned that BPG is abundantly present in erythrocytes to greatly reduce the affinity of hemoglobin for oxygen. When 2,3-BPG binds to deoxyhemoglobin, it acts to stabilize the low oxygen affinity state (T state) of the oxygen carrier. What would happen to hemoglobin if the BPG were removed? Would our body still be able to efficiently deliver oxygen to the tissues?arrow_forward
- What kind of Oxygen-Dissociation curve do you expect when carbon monoxide attaches to hemoglobin molecules ? ------------------------------------------- Why do we observe this change from a normal oxygen dissociation curve ? And why is this change hazardous ? Please Answer All Question, Don't Answer only One Question if you are real expert ! Don't Spam or copy from Other websites. It's Urgent Thankyou and All the Best :)arrow_forwardin thalassemia, a type of anemia, the hemoglobin molecule is malformed. The malformation prevents hemoglobin from carrying and delivering the correct amount of oxygen to the cells. Which important physiological concept does this example illustrate?arrow_forwardWhy is oxygen efficiently transferred from hemoglobin in theblood to myoglobin in the muscles?arrow_forward
- Why is impairment of hemoglobin dangerous?arrow_forwardIn addition to O2 binding, changes in other chemical conditions can result in changes in hemoglobin structure and function. Increases in blood H+ result in oxygen binding curves for hemoglobin that are shifted to the right. The effect of H+ can be understood in terms of the equilibrium:H-Hb+ + O2 → Hb-O2 + H+How does the difference in pH in the lungs and tissues help hemoglobin do its job of delivering oxygen? Use the equilibrium equation in your argument.arrow_forward“The binding of oxygen to hemoglobin exhibits positive cooperativity.” Explain brieflyarrow_forward
- Why does hemoglobin have high affinity for oxygen in arterial blood and lower affinity in capillaries beds? Explain in terms of blood oxygen pressure.arrow_forwardDescribe the two basic parts of a hemoglobin molecule.Which part is associated with iron? What gases aretransported by each part?arrow_forward
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