WHAT IS LIFE? A GUIDE TO BIO 3E+LAUNCHPA
3rd Edition
ISBN: 9781319103316
Author: PHELAN
Publisher: Macmillan Higher Education
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Chapter 21, Problem 16MC
Summary Introduction
Introduction:
Hemoglobin is the molecule that binds oxygen.
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Which 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.
Which of the following statements is true about hemoglobin?
a.hemoglobin
b. Each hemoglobin molecule is made up of one alpha and one beta chain polypeptide.
C. All that is needed to bind oxygen is a molecule of heme.
D. Each hemoglobin molecule can carry four oxygen molecules.
Which 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 myoglobin
Chapter 21 Solutions
WHAT IS LIFE? A GUIDE TO BIO 3E+LAUNCHPA
Ch. 21 - Prob. 1SACh. 21 - Prob. 2SACh. 21 - Prob. 3SACh. 21 - Prob. 4SACh. 21 - Prob. 5SACh. 21 - Prob. 6SACh. 21 - Prob. 7SACh. 21 - Prob. 8SACh. 21 - Prob. 9SACh. 21 - Prob. 10SA
Ch. 21 - Prob. 11SACh. 21 - Prob. 12SACh. 21 - Prob. 13SACh. 21 - Prob. 14SACh. 21 - Prob. 15SACh. 21 - Prob. 16SACh. 21 - Prob. 17SACh. 21 - Prob. 18SACh. 21 - Prob. 1MCCh. 21 - Prob. 2MCCh. 21 - Prob. 3MCCh. 21 - Prob. 4MCCh. 21 - Prob. 5MCCh. 21 - Prob. 6MCCh. 21 - Prob. 7MCCh. 21 - Prob. 8MCCh. 21 - Prob. 9MCCh. 21 - Prob. 10MCCh. 21 - Prob. 11MCCh. 21 - Prob. 12MCCh. 21 - Prob. 13MCCh. 21 - Prob. 14MCCh. 21 - Prob. 15MCCh. 21 - Prob. 16MCCh. 21 - Prob. 17MCCh. 21 - Prob. 18MC
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- Which of the following is incorrect? a. Hemoglobin transports oxygen through the blood from the lungs to the tissues Ob. None; all the other choices are correct c. Hemoglobin transports H+ through the blood from the tissues to the lungs O d. Lower pH increases hemoglobin's O₂-binding affinityarrow_forwardWhich molecule has the greatest ability to stabilize the deoxy state of hemoglobin? Select one: a. all have equal ability b. ВPG C. CO d. H e. Co2arrow_forwardWhich of the following describe(s) a characteristic or function of hemoglobin?a. Hemoglobin consists of four chains of amino acids.b. A hemoglobin molecule contains four iron ions to carry oxygen.c. In addition to transporting oxygen, hemoglobin molecules carry carbon dioxide and hydrogen ions.d. Hemoglobin is a protein found in all formed elements.e. There are four hemoglobin molecules in each red blood cell.arrow_forward
- All of the following are accurate statements about hemoglobin except a. hemoglobin carries oxygen on the Fe ion. b. hemoglobin carries carbon dioxide on the globin. c. hemoglobin carries only a small portion of the total carbon dioxide in the blood (less than 25%). d. hemoglobin releases oxygen at the level of the cell, making hemoglobin more saturated.arrow_forwardIf 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_forwardWhich of the following statements is INCORRECT about how the components of hemoglobin are recycled? a. Iron ions are either stored in a phagocytic cell or circulate in the blood, bound to transferrin (a plasma protein). b. Each heme is stripped of its iron and converted to bilirubin, then excreted in bile. c. The alpha and beta chains are released into the bloodstream for use by other cells. d. Hemoglobin can be recycled only if phagocytized by macrophages.arrow_forward
- Which of the following stabilize the hemoglobin quaternary structure of low-affinity to oxygen molecules? Group of answer choices a. CO b. CO2 c. bisphosphoglycerate d. H+arrow_forwardCarbon monoxide poisoning occurs because a. CO2 and O2 compete for the same binding site on hemoglobin. b. CO and CO2 compete for the same binding site. c. Hemoglobin in the presence of CEO destroys the oxygen. d. All answers are correctarrow_forwardWhich 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_forward
- Which of the following scenariosare correct?Select all that apply A. High levels of PCO2will cause loading of O2ontohemoglobin. B. An increase in pH will causeO2to unload from hemoglobin. C. High PO2levels will increase saturation of Hb with O2. D. An increase in bodytemperature will cause O2to unload from hemoglobin.arrow_forwardWhat 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_forwardWhich 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.arrow_forward
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