Study Guide for Campbell Biology
11th Edition
ISBN: 9780134443775
Author: Lisa A. Urry, Michael L. Cain, Steven A. Wasserman, Peter V. Minorsky, Jane B. Reece, Martha R. Taylor, Michael A. Pollock
Publisher: PEARSON
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Chapter 42, Problem 26TYK
Summary Introduction
Introduction: The exchange of gases is the process of transport of oxygen to the tissues from the lungs and the removal of carbon dioxide from the tissues to the lungs. The oxygen is transported by the protein hemoglobin present in the RBC cells of the blood. The transport of gases occurs between the alveoli of the lungs and the capillaries present in the walls of the alveoli. When one oxygen molecule gets transported to the blood simultaneously one carbon dioxide molecule blows out of the lungs.
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Which statement is true for the heme group present myoglobin:
a.
Oxygen binding to heme group is influenced by serine residues within proteins’ sequences.
b.
Oxygen binding to heme can become irreversible as a result of interaction with certain protein residues.
c.
Oxygen reversibly binds to the heme prostetic group and this binding is influenced by histidine residues within the myoglobin sequence.
d.
The heme group dissociates from Mb after oxygen is released.
The graph below shows the O₂-binding curves for myoglobin (Mb) and hemoglobin
(Hb).
a.
100
80
60
40
20
0
0
20
40 60 80 100
pO₂ (torr)
a. Use the graph to determine the Kd of myoglobin for O₂ (show your approach).
Write that in the provided space.
b. What is the difference between myoglobin and hemoglobin that cause the O₂-
binding curves to so be different? Answer in the provided space.
c. Why is it important that hemoglobin has these particular O₂-binding
characteristics? Answer in the provided space.
YO₂
Why is the decreased affinity of fetal hemoglobin for BPG advantageous?
With fewer BPG molecules bound to heme, there are more heme residues available for O2 binding.
O A.
B. Decreased BPG binding biases the fetal hemoglobin toward the R state.
C. More free BPG is available to bind to adult hemoglobin, resulting in a shift to the R state.
BPG is more available to bind to fetal myoglobin. helping to release O2 in fetal muscle tissue.
D.
47
Chapter 42 Solutions
Study Guide for Campbell Biology
Ch. 42 - Prob. 1IQCh. 42 - Prob. 2IQCh. 42 - In the following diagram of a mammalian...Ch. 42 - a. Name the valve between an atrium and ventricle....Ch. 42 - Prob. 5IQCh. 42 - Prob. 6IQCh. 42 - Prob. 7IQCh. 42 - What lifestyle choices have been correlated with...Ch. 42 - Prob. 9IQCh. 42 - Prob. 10IQ
Ch. 42 - Prob. 11IQCh. 42 - Identify the labeled structures in the following...Ch. 42 - Prob. 2SYKCh. 42 - Prob. 1TYKCh. 42 - Prob. 2TYKCh. 42 - Prob. 3TYKCh. 42 - Prob. 4TYKCh. 42 - During diastole, a. blood fills the atria and...Ch. 42 - Prob. 6TYKCh. 42 - As a general rule, blood leaving the right...Ch. 42 - The nurse tells you that your blood pressure is...Ch. 42 - Blood flows more slowly in arterioles than in...Ch. 42 - Prob. 10TYKCh. 42 - Prob. 11TYKCh. 42 - Prob. 12TYKCh. 42 - Prob. 13TYKCh. 42 - Exchange between the blood and the tissues of the...Ch. 42 - Which of the following processes would tend to...Ch. 42 - Prob. 16TYKCh. 42 - Prob. 17TYKCh. 42 - Prob. 18TYKCh. 42 - Prob. 19TYKCh. 42 - Prob. 20TYKCh. 42 - What do the alveoli of mammalian lungs, the gill...Ch. 42 - Prob. 22TYKCh. 42 - Prob. 23TYKCh. 42 - Prob. 24TYKCh. 42 - Prob. 25TYKCh. 42 - Prob. 26TYK
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- Which of the following is true about the T (tense) -->R (relaxed) transition of hemoglobin? A. The T state of hemoglobin binds oxygen with a higher affinity than the R state. B. The binding of O2 to a subunit T state can cause the transition of other subunits to the R state. C. The T state has a narrower pocket between b subunits than does the R state. D. When hemoglobin undergoes the T--> R transition, the structures of the individual subunits change dramatically.arrow_forwardWhich is/are false? a. Carbaminohemoglobin is hemoglobin bound to carbon dioxide b. In the lungs, the oxyhemoglobin saturation curve undergoes a 'left shift' c. At a PO2 of 10 mmHg, there is more deoxyhemoglobin in blood that oxyhemoglobin d. Higher temperatures and lower pH cause hemoglobin to bind more readily with oxygen than in conditions of lower temperatures and higher pHarrow_forwardIn the absence of 2,3-bisphosphoglycerate, the binding of oxygen by hemoglobin: a. is characterized by cooperativity b. resembles that of myoglobin c. binds at the end of the hemoglobin molecule d. is stabilized as the deoxy conformation of hemoglobin for the release into capillariesarrow_forward
- Which of the following statements about the I state of hemoglobin is FALSE? a, iron ion is pulled to the plane of the heme ring b. stabilized by ion pairing at the dimers interface c. 2,3-bisphosphoglycerate shifts the RT equilibrium towards the T state O d. tense state of hemoglobinarrow_forwardIn mammals, the developing fetus obtains O₂ from its mother's blood via the placenta. For this to occur... A. The fetal hemoglobin must have a higher Pso than the maternal hemoglobin B. The O₂ equilibrium curve of the fetal hemoglobin must be left-shifted with respect to the curve for the maternal hemoglobin C. The maternal hemoglobin must have a higher O₂ binding affinity than the fetal hemoglobin D. The O₂ carrying capacity of the fetal hemoglobin must be greater than that of the maternal hemoglobin E. None of the abovearrow_forwardWhich of the following is true about the proximal histidine of hemoglobin? A. It forms a hydrogen bond with bound oxygen. B. It is bonded to the Fe2+ atom coordinated by heme C. It binds oxygen D. It is not consumed in myoglobinarrow_forward
- What is the biological advantage to the sigmoidal binding curve of hemoglobin for oxygen? A. It ensures that hemoglobin has a high affinity for oxygen. B. It allows hemoglobin to bind oxygen irreversibly. C. It ensures that hemoglobin can bind oxygen only weakly. D. It allows hemoglobin to shift between low and high affinities for oxygen.arrow_forwardMyoglobin benefits muscle cells by ... A. binding with O2 just as strongly as hemoglobin does. B. releasing bound O2 at lower PO2 conditions than hemoglobin does. C. increasing the effectiveness of fast glycolytic muscle fibers used in short bursts. D. contributing to the elasticity of flight muscle in birds. E. using hemoglobin as a reserve source of oxygen.arrow_forwardWhich 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.arrow_forward
- If the blood lacked red blood cells but the lungs were functioning normally, A. The arterial PO2 would be normal. B. The oxygen content of arterial blood would be normal. C. Both A and B would apply. D. Neither A nor B would apply Which of the following would be most affected by a decrease in the affinity of hemoglobin for oxygen? A. Arterial PO2 B. Arterial percent oxyhemoglobin saturation C. Venous oxyhemoglobin saturation D. Arterial PCO2arrow_forwardA. The affinity of oxygen to hemoglobin in Baguio City B. The affinity of oxygen to hemoglobin at sea level O A. The FIRST quantity is the larger of the 2. O B. The SECOND quantity is the larger of the 2. O C. The two quantities are EQUAL in size A. The rate at which O2 detaches from hemoglobin when temperature is high B. The rate at which O2 detaches from hemoglobin when temperature is low O A. The FIRST quantity is the larger of the 2. O B. The SECOND quantity is the larger of the 2. C. The two quantities are EQUAL in sizearrow_forwardThe Bohr effect related to A. the ability of Hb to bind 02 in the presence of BPG. the ability of myoglobin to expel protons when binding 02. B. the ability of Hb to "take up" protons when binding 02. C. the ability of Hb to release protons when binding O2. D. O E. BPG ionization at 30 torr (the pO2 in veins).arrow_forward
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