Campbell Biology (10th Edition)
10th Edition
ISBN: 9780321775658
Author: Jane B. Reece, Lisa A. Urry, Michael L. Cain, Steven A. Wasserman, Peter V. Minorsky, Robert B. Jackson
Publisher: PEARSON
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Chapter 2.1, Problem 3CC
Summary Introduction
To evaluate: The effects of iron deficiency in the human body.
Concept introduction:
Iron is a trace element. Although, it is required in small quantity, it is essential for the maintenance of human body. It is a component of hemoglobin protein present in red blood cells (RBCs).
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Recall from your BI110 class that metabolically active tissues produce CO2 as a by-product of cellular respiration. Those metabolically active tissues require the O2 that is brought by hemoglobin for the same process (cellular respiration). Explain why the effect of pH on hemoglobin’s affinity for oxygen is consistent with delivering it to actively metabolizing tissues. (Hint: think about what effect the presence of CO2 has on the tissues…)
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O, saturation curve is shown beloww for hemoglobin at various pHs. Detail this Bohr
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in delivery of 02 to areas of higher demand.
100
Myoglobin
80-
pH 7.6
60
pH 7.4
pll 7.2
40-
pH 7.0
pH 6.8
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Venous
0-
0.
20
10
60
80
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Chapter 2 Solutions
Campbell Biology (10th Edition)
Ch. 2.1 - MAKE CONNECTIONS Explain how table salt has...Ch. 2.1 - Is a trace element an essential element? Explain.Ch. 2.1 - Prob. 3CCCh. 2.1 - MAKE CONNECTIONS Explain how natural selection...Ch. 2.2 - Prob. 1CCCh. 2.2 - A nitrogen atom has 7 protons, and the most common...Ch. 2.2 - Prob. 3CCCh. 2.2 - Prob. 4CCCh. 2.3 - Why does the structure H C = C H fail to make...Ch. 2.3 - What holds the atoms together in a crystal of...
Ch. 2.3 - What holds the atoms together in a crystal of...Ch. 2.4 - Prob. 1CCCh. 2.4 - Which type of chemical reaction, if any, occurs...Ch. 2.4 - WHAT IF? Write an equation that uses the products...Ch. 2 - Prob. 2.1CRCh. 2 - DRAW IT Draw the electron distribution diagrams...Ch. 2 - In terms of electron sharing between atoms,...Ch. 2 - What would happen to the concentration of products...Ch. 2 - Level 1: Knowledge/Comprehension 1. In the term...Ch. 2 - Compared with 31P, the radioactive isotope 32P has...Ch. 2 - The reactivity of an atom arises from (A) the...Ch. 2 - Which Statement is true of all atoms that are...Ch. 2 - Which of the following statements correctly...Ch. 2 - Prob. 6TYUCh. 2 - The atomic number of sulfur is 16. Sulfur combines...Ch. 2 - What coefficients must be placed in the following...Ch. 2 - DRAW IT Draw Lewis dot structures for each...Ch. 2 - EVOLUTION CONNECTION The percentages of naturally...Ch. 2 - Prob. 11TYUCh. 2 - Prob. 12TYUCh. 2 - Prob. 13TYU
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- 2. (a) The binding site of 2,3-bisphosphoglycerate (BPG) (red stick figure) in the deoxyhemo- globin molecule is illustrated below. Note that the two phosphate groups and the carboxylate group of the BPG molecule confer strong, negative electrostatic character to the molecule. B₁-subunit 1. 2. 3. 5. 6. B₁ (b) Mutant Hemoglobin Hb Raleigh Hb Helsinki The mutant hemoglobins listed below each have a mutant amino acid in the ß-subunit directly in or in the vicinity of the BPG binding site. Rank the affinity of the following mutant hemoglobins for binding BPG (red stick figure above).. Explain your reasoning. The notation, for instance, as given for Hb Raleigh Val(31)Ala means that Val-1, the first amino acid residue of the ß-subunit, has been substituted by Ala. Hb Rahere Hb Rancho Mirage Hb Little Rock B₂ Hb Ohio Mutation Val (31)Ala Lys(382) Met Lys(382)) Thr His(143)Asp His(3143)Gln a-NHẠ Ala(142)Asp His 2 His 143 BPG His 143 Lys 82 His 2 Rank the affinity of the mutant hemoglobins for…arrow_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_forwardGive typed full explanationarrow_forward
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