Biology: The Unity and Diversity of Life (MindTap Course List)
14th Edition
ISBN: 9781305073951
Author: Cecie Starr, Ralph Taggart, Christine Evers, Lisa Starr
Publisher: Cengage Learning
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Chapter 38, Problem 2CT
Summary Introduction
To explain: How does the fetal hemoglobin’s higher affinity towards oxygen benefit a fetus.
Concept introduction: Fetal hemoglobin is the main source of oxygen transport in the human fetus. It is present during the last seven months of the development of the uterus. It persists in the new born until 6 months. In adults, the fetal hemoglobin can be reactivated pharmacologically and can be used in the treatment of diseases.
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in 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?
In 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.
Which of the following situations occurs if a person's blood becomes more alkaline?
A.
Hemoglobin molecules retain less oxygen per heme group under alkaline conditions than they do at neutral pH or under acidic conditions.
B.
Hemoglobin molecules give up oxygen more readily under alkaline conditions than they do under neutral pH or under acidic conditions.
C.
Hemoglobin molecules change shape and begin to lose oxygen molecules.
D.
Hemoglobin molecules retain oxygen more readily under alkaline conditions than they do at neutral pH or under acidic conditions.
E.
There is no change in hemoglobin's oxygen-binding affinity under alkaline conditions when compared to blood at neutral pH or under acidic conditions.
Chapter 38 Solutions
Biology: The Unity and Diversity of Life (MindTap Course List)
Ch. 38 - Respiratory proteins such as hemocyanin _____. a....Ch. 38 - In a _______, air flows continually across the...Ch. 38 - Prob. 3SQCh. 38 - In human lungs, gas exchange occurs at the ______....Ch. 38 - Prob. 1DAACh. 38 - Prob. 2DAACh. 38 - Prob. 3DAACh. 38 - Which holds the most dissolved oxygen? a. warm,...Ch. 38 - When you breathe quietly, inhalation is _______...Ch. 38 - Prob. 7SQ
Ch. 38 - Prob. 8SQCh. 38 - Most oxygen transported in human blood _______. a....Ch. 38 - Prob. 10SQCh. 38 - In fish gills, blood and water move ________. a....Ch. 38 - ______ in arteries sense changes in the acidity of...Ch. 38 - Prob. 13SQCh. 38 - The diaphragm is a ______ muscle. a. smooth b....Ch. 38 - Prob. 15SQCh. 38 - Prob. 1CTCh. 38 - Prob. 2CT
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- In 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_forwardAfter 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?arrow_forwardWhat is the difference in the quaternary structure between fetal hemoglobin and adult hemoglobin? Which one can carry more oxygen?arrow_forward
- Reduction in pH of blood will -------------------------- (descrease/increase) the affinity of hemoglobin with oxygen.arrow_forwardThe ability of hemoglobin to bind oxygen decreases with decreasing oxygen concentration and also decreases with increasing carbon dioxide concentration. What effect do these phenomena have on the delivery of oxygen to tissues?arrow_forwardWhich of the following statements about oxygen transport is TRUE. Increases in temperature and decreases in pH cause myoglobin to release oxygen to improve delivery to the hemoglobin in muscles. A molecule of myoglobin has higher oxygen binding capacity than a molecule of hemoglobin. Myoglobin has a higher oxygen affinity than does hemoglobin. Fetal hemoglobin has a lower affinity for oxygen than maternal hemoglobin, which makes it better suited to extract oxygen from the maternal circulation.arrow_forward
- Compare and contrast adult hemoglobin and fetal hemoglobin?arrow_forwardCarbon monoxide is a colorless, odorless gas produced by combustion, including the burning of tobacco. If inhaled, it binds tightly to the oxygen-binding sites on hemoglobin. Why does exposure to low levels of carbon monoxide produce symptoms like those of anemia?arrow_forwardCarbon monoxide (CO) is a colourless, odourless gas that result from the burning of hydrocarbons, such as in a poorly functioning furnace or vehicle emissions. CO can bind with hemoglobin to form carboxyhemoglobin. Hemoglobin's affinity for CO is 200 times greater than its affinity for oxygen. The initial symptoms of carbon monoxide poisoning are flu-like, such as dizziness, headache and vomiting. However, when left unchecked, CO poisoning can result in unconsciousness, loss of blood flow to the vital organs and, eventually, death. (Source: Bleecker, M.L. (2015). Carbon Monoxide Intoxication. Handbook of Clinical Neurology. Elsevier B.V.) 5. Name the gases normally carried by hemoglobin in the body. Using your knowledge of the circulatory and respiratory systems, provide a possible explanation for the symptoms of carbon monoxide poisoning.arrow_forward
- Which of the following describe(s) a characteristic or function of hemoglobin?a. Hemoglobin consists of four chains of amino acids.b. A hemoglobin molecule contains four iron ions to carry oxygen.c. In addition to transporting oxygen, hemoglobin molecules carry carbon dioxide and hydrogen ions.d. Hemoglobin is a protein found in all formed elements.e. There are four hemoglobin molecules in each red blood cell.arrow_forwardAnswer the following questions about hemoglobin. The number of high affinity binding sites in the R form of hemoglobin is .The number of low affinity binding sites in the R form of hemoglobin is .The number of O2 molecules that need to bind to convert hemoglobin from the T to R form is .The number of high affinity binding sites in the T form of hemoglobin is .The number of low affinity binding sites in the T form of hemoglobin isarrow_forwardWhich of the following statements is true about hemoglobin? a.hemoglobin b. Each hemoglobin molecule is made up of one alpha and one beta chain polypeptide. C. All that is needed to bind oxygen is a molecule of heme. D. Each hemoglobin molecule can carry four oxygen molecules.arrow_forward
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