Human Biology : Concepts and Current Issues - With Access
7th Edition
ISBN: 9780321874856
Author: Johnson
Publisher: PEARSON
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Chapter 7, Problem 4AWK
Summary Introduction
To review:
The variable responsible for lowering the pH level in metabolically active cells that causes the release of oxygen from the red blood cells (RBCs).
Introduction:
RBC is the cellular component of blood, which is responsible for carrying oxygen from lungs and supplies it to the body cells. Oxygen is the key ingredient that is required for the
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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 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
The following statement describes which level of structure of the hemoglobin molecule?
"Each chain is stabilized by electrostatic interactions between -COO- and -NH3+ of amino acid side chains."
Primary
Second
Tert
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Chapter 7 Solutions
Human Biology : Concepts and Current Issues - With Access
Ch. 7 - Prob. 1QCCh. 7 - Prob. 2QCCh. 7 - Describe the functions of blood.Ch. 7 - Prob. 2CRCh. 7 - Explain how the production of red blood cells is...Ch. 7 - Prob. 4CRCh. 7 - Prob. 5CRCh. 7 - Prob. 6CRCh. 7 -
7. Describe the mechanism of hemostasis.
Ch. 7 - Prob. 8CR
Ch. 7 - Prob. 9CRCh. 7 - Prob. 10CRCh. 7 - Prob. 1TYCh. 7 - Prob. 2TYCh. 7 - Prob. 3TYCh. 7 - Prob. 4TYCh. 7 - Prob. 5TYCh. 7 -
6. A person with Type A- (A-negative) blood will...Ch. 7 - Prob. 7TYCh. 7 - Prob. 8TYCh. 7 - Prob. 9TYCh. 7 - Prob. 10TYCh. 7 -
11. Which white blood cells are present in the...Ch. 7 - Prob. 12TYCh. 7 - Prob. 13TYCh. 7 - Prob. 14TYCh. 7 - Prob. 15TYCh. 7 - Prob. 1AWKCh. 7 - Prob. 2AWKCh. 7 - Prob. 3AWKCh. 7 - Prob. 4AWKCh. 7 - Prob. 5AWKCh. 7 -
6. Coumadin is an anticoagulant drug that is...
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- Hemoglobin will bind oxygen and release CO2 in places where there is a higher concentration of O2, lower concentration of CO2, lower temperature and lower acidity (as it is in lungs) and will do the reverse – release oxygen and bind CO2 - in places where there is a lower concentration of O2, higher concentration of CO2, higher temperature and higher acidity (as it is in working muscles). True False While white blood cells never leave the circulation, red blood cells regularly leave it and travel by lymphatic system or find home in other tissues, e.g., lymph nodes, spleen, etc. True False Blood clotting (coagulation) is a complex process involving many factors and it exhibits positive feedback loops: many of the factors also stimulate production of their own precursors. B lymphocytes mature in the thymus while T lymphocytes mature in the bone marrow True False Antibodies are molecules on the surfaces of foreign…arrow_forwardWhy does hemoglobin have high affinity for oxygen in arterial blood and lower affinity in capillaries beds? Explain in terms of blood oxygen pressure.arrow_forwardThe ability of hemoglobin to bind oxygen decreases with decreasing oxygen concentration and also decreases with increasing carbon dioxide concentration. What effect do these phenomena have on the delivery of oxygen to tissues?arrow_forward
- Can all abnormal hemoglobin be diagnosed by electrophoresis ?Explain why or why not .arrow_forwardAnswer the following questions about hemoglobin. The number of high affinity binding sites in the R form of hemoglobin is .The number of low affinity binding sites in the R form of hemoglobin is .The number of O2 molecules that need to bind to convert hemoglobin from the T to R form is .The number of high affinity binding sites in the T form of hemoglobin is .The number of low affinity binding sites in the T form of hemoglobin isarrow_forwardWhat is the role of the heme prosthetic group in hemoglobin? A. The heme group coordinates the subunits of hemoglobin. B. The heme group binds one molecule of oxygen in the center of the hemoglobin protein. C. The heme group binds a molecule of oxygen for each subunit of hemoglobin. D. The iron atom in the heme group is needed to irreversibly bind oxygen.arrow_forward
- What is the major element found in hemoglobin that allows it to do its job?arrow_forwardCarbon monoxide binds to hemoglobin more readily than oxygen. Why is this dangerous?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_forward
- Match the descriptor in the left hand column to the type of molecule it describes listed in the right hand column.. Question 4 options: hemoglobin molecule with heme groups containing iron atoms in the reduced state to which carbon monoxide molecules are attached hemoglobin molecule with heme groups containing iron atoms in the reduced state to which oxygen molecules are attached hemoglobin molecule with heme groups containing iron atoms in the oxidized state to which no oxygen molecules can attach hemoglobin molecule with heme groups containing iron atoms in the reduced state to which no oxygen molecules are attached hemoglobin molecule with heme groups containing iron atoms in the reduced state and carbon dioxide molecules attached to amino acid residues of the globin chains 1. carbaminohemoglobin 2. carboxyhemoglobin 3. deoxyhemoglobin 4. methemoglobin 5. oxyhemoblobinarrow_forwardWhich of the following factors would increase the amount of oxygen discharged by hemoglobin to peripheral tissues? a. decreased amounts of DPG b. increased tissue PO2 c. decreased pH d. decreased temperature e. all of the abovearrow_forwardWhat is the name of the molecule when glucose is bound to hemoglobin? a. Glycohemoglobin b. Beta cell c. Glycosylated molecule d. RBC complexarrow_forward
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