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
expand_more
expand_more
format_list_bulleted
Concept explainers
Question
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).
Expert Solution & Answer
Want to see the full answer?
Check out a sample textbook solutionStudents have asked these similar questions
. 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
0.913
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 prediction
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…
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
Knowledge Booster
Learn more about
Need a deep-dive on the concept behind this application? Look no further. Learn more about this topic, biology and related others by exploring similar questions and additional content below.Similar questions
- In 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_forwardWhat 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_forward
- 3. (a) The (acid) Bohr effect is defined as the up- take of protons by hemoglobin molecules at pH ≤ 6.5 as O2 is dissociated from the protein in solution. Approxi- mately 0.6 mole protons are taken up for each mole of O2 released by normal human hemoglobin. The effect is seen as a "shift to the right" in the O2 dissociation curves with decrease in pH, indicating that the O2 binding affinity of Hb decreases at lower pH. On the right is a diagram compar- ing the pH dependence of the p50 values of Hb Deer Lodge [His(32)Arg] (filled symbols) and of HbA (- - -) in the absence of organic phosphates, i.e., “Stripped”, and in the presence of saturating concentrations of IHP. On the basis of the definition of the Bohr effect given above, explain why the data in the diagram reflect the Bohr effect for the two types of human hemoglobins. log p50 1.5 1.0 0.5 0.0 -0.5 5 6 stripped 7 pH +DPG 8 IHP 9 (b) The Bohr effect is generally decreased in Hb Deer Louge compared to that in HbA. Provide an…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_forward2. j The following plots show an oxygen binding curve for hemoglobin under a certain set of conditions. For each plot, sketch (with reasonable accuracy) a second curve showing how the binding of oxygen to hemoglobin would be altered by the change in conditions noted. a. Increase in pCO2 b. Dissociation of native Hb into aß dimers 1 0.8 0.8 0.6 Y 0.4 0.6 Y 0.4 0.2 0.2 po2 pO2arrow_forward
- What qualitative effect would you expect each of the following to have on the Ps0 of hemoglobin? (a) Increase in pH from 7.2 to 7.4 (b) Increase in Pco, from 20 to 40 mm Hg (c) Dissociation into monomer polypeptide chainsarrow_forward3)arrow_forwardA new oxygen transport protein that exhibits cooperative binding has been isolated and is beingstudied in the lab. Calculate the KD value if Y = 0.76 when pO2 = 18 torr (assume n = 2.5). Howdoes this compare to the KD value for hemoglobin? Does this protein bind more or less tightly tooxygen compared to hemoglobin?arrow_forward
- Why does the dissociation constant change for hemoglobin in high and low 02 concentrations? O Hemoglobin is a tetramer and subunits have decreased dissociation of 02 when a neighboring subunit has bound 02 O Hemoglobin is a monomeric protein with increased dissociation of 02 when a neighboring molecule has bound 02 O Hemoglobin is a tetramer and subunits have increased dissociation of 02 when a neighboring subunit has bound CO O Hemoglobin is a tetramer and subunits have increased dissociation of O2 when a neighboring subunit has bound O2arrow_forwardSolve all asaparrow_forwardChemistry Red cells have a volume of ~86 fL. If the concentration of hemoglobin in red cells is ~330 g/L and its Mr is 64,500 b) In the generation of a red cell, the synthesis of all the hemoglobin molecules of the cell takes about 40 h. How many hemoglobin molecules are synthesized in one second per red cell? c) How many subunits (monomers) of hemoglobin are produced in one minute?arrow_forward
arrow_back_ios
SEE MORE QUESTIONS
arrow_forward_ios
Recommended textbooks for you
- Biology: The Dynamic Science (MindTap Course List)BiologyISBN:9781305389892Author:Peter J. Russell, Paul E. Hertz, Beverly McMillanPublisher:Cengage LearningHuman Physiology: From Cells to Systems (MindTap ...BiologyISBN:9781285866932Author:Lauralee SherwoodPublisher:Cengage Learning
Biology: The Dynamic Science (MindTap Course List)
Biology
ISBN:9781305389892
Author:Peter J. Russell, Paul E. Hertz, Beverly McMillan
Publisher:Cengage Learning
Human Physiology: From Cells to Systems (MindTap ...
Biology
ISBN:9781285866932
Author:Lauralee Sherwood
Publisher:Cengage Learning