LABORATORY MANUAL FOR HUMAN ANATOMY & PH
4th Edition
ISBN: 9781260254426
Author: Martin
Publisher: MCG
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Chapter 42, Problem 2PL
Summary Introduction
Introduction:
Hemoglobin is a protein molecule. It is responsible for binding oxygen in the Red blood cells. The hemoglobin molecule is composed of four protein subunits. They are two alpha and two beta subunits. Each subunit containing a heme molecule with an atom of iron. Each iron binds to one oxygen molecule As a result; each Hemoglobin molecule can bind to as many as four oxygen molecules.
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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
Which 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.
Chapter 42 Solutions
LABORATORY MANUAL FOR HUMAN ANATOMY & PH
Ch. 42 - Prob. 1PLCh. 42 - Prob. 2PLCh. 42 - Prob. 3PLCh. 42 - Prob. 4PLCh. 42 - Coagulation should normally occur within a. 10...Ch. 42 - Prob. 6PLCh. 42 - A normal blood total cholesterol level is less...Ch. 42 - The high-density lipoproteins (HDLs) are sometimes...Ch. 42 - Prob. 1.1CTCh. 42 - Prob. 2.1A
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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.arrow_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_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
- People suffering with sickle cell anemia have a structural defect in hemoglobin (HB). The major reason for this structural change is mutation of glutamic acid to valine. This leads to a Exposure of polar amino acids, leading to disintegration of hemoglobin. b Burying of polar amino acids, leading to disintegration of hemoglobin. c Exposure of non-polar amino acids leading to long fiber formation. d Burying of non-polar amino acids thereby increasing hydrophobic interactions and formation of long fibres.arrow_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_forwardAll 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_forward
- Match the following with its function: plasma protein that creates osmotic pressure that prevents fluids from leaking out of blood vessels (prevents edema) A. albumin B. fibrinogen plasma protein that helps cause blood clotting C. platelets v Formed element that causes blood clotting. D. white blood cells Formed element important in the immune E. red blood cells system. F. hemoglobin v formed element that carries oxygen v protein that binds to oxygenarrow_forwardWhich of the components of hemoglobin is correctly matched with itsfate following the destruction of a red blood cell?a. heme—reused to form a new hemoglobin moleculeb. globin—broken down into amino acidsc. iron—mostly secreted in biled. All of these are correctarrow_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_forward
- Which of the following is incorrect about 2,3-bisphosphoglycerate (BPG)? It is highly (-) charged b. It prevents binding of O₂ to hemoglobin Oc. It binds only to the relaxed (oxy) conformation of hemoglobin Od. It binds in the space between the four subunits of hemoglobin a.arrow_forwardWhich 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_forwardHaemoglobin... A. Consists of one or more globin proteins, each with a copper-containing heme group B. Increases the concentration of O₂ in the blood C. Is present only in vertebrates D. Is located within "pink cells" that circulate in the blood E. All of the abovearrow_forward
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