Campbell Biology (11th Edition)
11th Edition
ISBN: 9780134093413
Author: Lisa A. Urry, Michael L. Cain, Steven A. Wasserman, Peter V. Minorsky, Jane B. Reece
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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Chapter 2 Solutions
Campbell Biology (11th 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 - Compare an element and a Compound.Ch. 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 - SCIENTIFIC INQUIRY Female luna moths (Actias luna)...Ch. 2 - Prob. 12TYUCh. 2 - Prob. 13TYU
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- Hemoglobin from different species can have different numbers of subunits. Let's consider three hemoglobin molecules: n = 1, n = 4, and n = 8, where each subunit has an oxygen P50 = 30 torr. (Recall that Pso is essentially a Kp and that oxygen partial pressure (torr) is directly proportional to concentration.) Which molecule transports the most O2 between the lungs (pO2 = 100 torr) and peripheral tissues (pO2 = 30 torr)? Please justify your answer.arrow_forward. Oxygen binding by the hemocyanin of the shrimp Callianassa has been measured. Using the following data, prepare a Hill plot and determine (a) Pso, (b) h (the Hill coefficient), and (c) the minimum number of oxygen binding sites on the protein molecule. Poz (mm Hg) Yoz Po, (mm Hg) Yo2 1.1 0.003 136.7 0.557 7.7 0.019 166.8 0.673 10.7 0.035 203.2 0.734 31.7 0.084 262.2 0.794 71.9 0.190 327.0 0.834 100.5 0.329 452.0 0.875 123.3 0.487 736.7 0.913arrow_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
- One of the molecules listed below is effective in reducing O2 affinity of human Hb in the absence of BPG: (1) Glucose 6-phosphate (2) Inositol hexaphosphate (3) Maleic acid (4) Lactate (5) Arginine - Interestingly, this molecule plays the role of BPG in bird and turtle hemoglobin. A) Write the chemical structure of each molecule mentioned above. (B) Predict what molecule is most effective in preventing O2 binding to Hb. In 20 words or less explain the rationale for your predictionarrow_forward2. (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_forward
- Give typed full explanationarrow_forwardIn an experiment, hemoglobin is dissociated in a buffer and a subunit is isolated to study for its oxygen binding affinity. (i) What is the shape of the oxygen dissociation curve is expected in the experiment?Explain why. (ii) Is the Km of the isolated subunit higher or lower than the Km of an intact hemoglobin?arrow_forwarde 1.0 0.5- 0 6. Answer the questions below about hemoglobin and myoglobin. a. Sketch and label the binding curves of Mb, Hb, and Hb below. pº₂ b. In the scenarios below for Hb, indicate what effect they would have on the binding curve and give a brief explanation? Scenario Decrease in the concentration of carbon dioxide (CO₂) Distal histidine (the histidine that aids in molecular oxygen binding) mutation to phenylalanine High heat and extreme pH changes Predict if the normal binding curve of Hb will shift right (Hbt), left (HbⓇ), completely to Mb, or no longer bind oxygen completely? Brief Explanationarrow_forward
- a. How many subunits does hemoglobin have? What are their conventional names? b. Identify the oxygen binding sites on hemoglobin. How many oxygens can one molecule of hemoglobin bind? How many oxygens can one subunit of hemoglobin bind? c. Identify the central cavity of hemoglobin. Is it the same or different than the oxygen binding site of hemoglobin?arrow_forwardWhich form of human hemoglobin may be present in some adults, but not in the embryo or the fetus? two a-globin chains (alpha) and two e-globin chains (epsilon) two b-globin chains (beta) and two g-globin chains (gamma) two e-globin chains (epsilon) and two z-globin chains (zeta) two z-globin chains (zeta) and two g-globin chains (gamma) two d-globin chains (delta) and two a-globin chains (alpha)arrow_forwardGive answer all questions with explanationarrow_forward
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