Campbell Biology, Books a la Carte Plus Mastering Biology with eText -- Access Card Package (10th Edition)
10th Edition
ISBN: 9780133922851
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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Chapter 2 Solutions
Campbell Biology, Books a la Carte Plus Mastering Biology with eText -- Access Card Package (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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- how does high pressure O2 treat CO poisoning?arrow_forwardHemoglobin 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_forward
- What would happen in terms of pH, T to R state stability, and oxygen-carrying capacity if hemoglobin's Arg141 was replaced with Asp?arrow_forwardOne 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_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
- Which 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_forwardWhat is the allosteric effect on O2 binding to the second subunit of hemoglobin after the first subunit binds after O2 binding? to 02? What state would hemoglobin be O A decrease in affinity of hemoglobin for 02: T-State O An increase in affinity of hemoglobin for O2: T-State An increase in affinity of hemoglobin for 02; R-State O A decrease in affinity of hemoglobin for O2; R-Statearrow_forward
- What qualitative effect would you expect each of the following to have onthe P50 of hemoglobin?(a) Increase in pH from 7.2 to 7.4(b) Increase in PCO2 from 20 to 40 mm Hg(c) Dissociation into monomer polypeptide chains(d) Decrease in 2,3-BPG concentration from 7 mM to 5 mM in red cells.arrow_forwardA team of biochemists uses genetic engineering to modify the interface region between hemoglobin subunits. The resulting hemoglobin variants exist in solution primarily as αβ dimers (few, if any, α2β2 tetramers form). Are these variants likely to bind oxygen more weakly or more tightly? Explain your answer.arrow_forwardWhich of the following statements is false concerning the structure of hemoglobin? a. The binding of BPG stabilizes the T-state of Hb b. The R-state of Hb is favored under environments of high concentrations of O2 c. Hemoglobin's affinity for oxygen increases as protons ionize from the N-terminal tails d. Hemoglobin is stabilized in the low affinity state in the presence of high concentration of protons e. Hemoglobin favors the R-state in basic environmentsarrow_forward
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