Bundle: Human Biology, Loose-leaf Version, 11th + MindTap Biology, 1 term (6 months) Printed Access Card
11th Edition
ISBN: 9781305616660
Author: Cecie Starr, Beverly McMillan
Publisher: Cengage Learning
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Chapter 8, Problem 3RQ
Summary Introduction
To determine: The missing labels to the given diagram of hemoglobin and mention the factors that affect the affinity of hemoglobin to bind with oxygen.
Introduction: Hematologic system comprises blood, blood vessels, and blood-forming organs. Blood is a fluid connective tissue that carries oxygen, glucose, and nutrients throughout the body. It mainly consists of four types of components, namely red blood cells (RBCs), white blood cells (WBCs), plasma, and platelets.
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Sketch out the binding site of Hemoglobin with oxygen bound . ( You can abstract the Heme ring out i.e. not draw each chemical bond). Please label both imported HIS residues.
I am eating a snack as I type this question. My body is breaking down the food to provide energy
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acidic byproduct could be produced, decreasing the the pH in my muscles.
a) What effect will this have on the structure of hemoglobin. (Briefly describe. No more than 2-3
sentences.)
b) What effect does this have on the Pso of hemoglobin?
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.
oxyhemoblobin
Chapter 8 Solutions
Bundle: Human Biology, Loose-leaf Version, 11th + MindTap Biology, 1 term (6 months) Printed Access Card
Ch. 8 - Prob. 1RQCh. 8 - What are the cellular components of blood? Where...Ch. 8 - Prob. 3RQCh. 8 - What is an agglutination response? How can it be...Ch. 8 - Prob. 5RQCh. 8 - Prob. 1SQCh. 8 - Prob. 2SQCh. 8 - Prob. 3SQCh. 8 - In the lungs, the main factor in boosting the...Ch. 8 - Which of the following statements about red blood...
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- What is oxyhemoglobin? Where does it form?arrow_forwardWrite the reversible reaction between hemoglobin and oxygen.arrow_forwardIn addition to O2 binding, changes in other chemical conditions can result in changes in hemoglobin structure and function. Increases in blood H+ result in oxygen binding curves for hemoglobin that are shifted to the right. The effect of H+ can be understood in terms of the equilibrium:H-Hb+ + O2 → Hb-O2 + H+How does the difference in pH in the lungs and tissues help hemoglobin do its job of delivering oxygen? Use the equilibrium equation in your argument.arrow_forward
- Contrast the structures of the proteins myoglobin and hemoglobin.arrow_forwardDescribe the structure of hemoglobin and How does the structure of hemoglobin allow it to combine with oxygen?arrow_forwardCompare the structure and function of hemoglobin and myoglobin. Which oxygen binding curve in the graph below belongs to myoglobin and which to hemoglobin? Please specify. Explain the effect of pH on oxygen binding to hemoglobin, and show on the graph in which direction the pH will shift if it falls below the physiological pH value (7.4).arrow_forward
- make or draw a model of a hemoglobin protein and label the different parts of the protein and its functionsarrow_forwardDescribe the structure of a hemoglobin molecule. Explain where O2 and CO2 are carried on a hemoglobin molecule?arrow_forwardHow many atoms of oxygen can be bound to a singlemolecule of hemoglobin?arrow_forward
- 1)Determine the properties of hemoglobin related to its chemical structure, function and color change during loading and unloading of oxygen. 2) To determine the hemoglobin content indicated by hematocrit.arrow_forwardSelect the hemoglobin variant(s) that are described by each statement. (a) The variant least likely to cause pathological symptoms. (b) The variant(s) likely to show pl values different from that of HbA on an isoelectric focusing gel. (c) The variant most likely to show a decrease in BPG binding and an increase in the overall affinity of the hemoglobin for oxygen. Answer Bank Hb Milwaukee Hb Cowtown Hb Memphis Hb Philly Hb Providence Hb Bibba HbSarrow_forwardWhat is the difference between oxyhemoglobin and reduced hemoglobin in terms of structure?arrow_forward
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