EBK HUMAN BIOLOGY
11th Edition
ISBN: 8220100545931
Author: MCMILLAN
Publisher: Cengage Learning US
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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
so that my muscles will continue to contract and I can continue to type. During this process, some
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
EBK HUMAN BIOLOGY
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_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_forwardBlood in our body changes color as a function of its oxygenation state. Given the spectral data below, calculate the absorbance of red light (600 nm) of fully oxygenated and deoxygenated blood. Using this data, determine what percentage of red light would go through a sample of blood that is 50% oxygenated. Assume the patient has a hemoglobin concentration of 10 mM and pathlength of 1 cm.arrow_forward
- Carbon monoxide binds to hemoglobin more readily than oxygen. Why is this dangerous?arrow_forwardUse the image below to answer this question and the three questions that follow: a) what is the correct description of the hemoglobin for Paul? b) Where is the + pole of the electrophoresis for the gel shown in the previous question? c) Refer to gel illustration above. Which of the following statements provides the best explanation for the difference in mobility of HbA and HbS? 1) HbA is larger in size than HbS 2) HbA is smaller in size than HbS 3) HbA has less negative charge than HbS under electrophoretic conditions used 4) HbA is smaller and more negatively charged under the electrophoretic conditions used 5) HbA is larger and has a less negative charge under the electrophoretic conditions used, whereas HbS is smaller and has a more negative chargearrow_forwardWhat color is deoxyhemoglobin? Why?arrow_forward
- Complete the following table about hemoglobin (Hb) characteristics. Оху-НЬ Deoxy-Hb Conformation [ Select ] [ Select ] ВPG [ Select ] [ Select ] > >arrow_forwardmake or draw a model of a hemoglobin protein and label the different parts of the protein and its functionsarrow_forwardExplain how the following conditions affect the structure and function of hemoglobin. Sickle cell anemia, fetal hemoglobin and lowed pHarrow_forward
- Select 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_forwarda) Hemoglobin accounts for 95% of the protein in red blood cells. If you Google the number of hemoglobin molecules in a RBC, most sources state 250-270 million hemoglobin molecules. If hemoglobin has a molecular weight of 67,000 Da, what is the concentration of hemoglobin in RBCs? Show your work and show your units. Use dimensional analysis to have your final answer in moles per liter. B) The hemoglobin molecule is nearly spherical with a diameter of 55 Angstroms. You can look at the 3D structure of human hemoglobin on the RCSB PDB website. Calculate the volume of a hemoglobin molecule, and can the number of hemoglobin molecules quoted in Question a actually fit into one red blood cell?arrow_forwardWhich five statements about hemoglobin and myoglobin structure are true? Each iron atom can form six coordination bonds. Two of these bonds are formed between iron and oxygen. Molecular oxygen binds reversibly to Fe²+ in heme. Heme is composed of an organic protoporphyrin component and a metal atom. By itself, heme is not a good oxygen carrier. It must be part of a larger protein to prevent oxidation of the iron atom. Each hemoglobin or myoglobin molecule can bind four oxygen molecules. Hemoglobin is a heterotetramer, whereas myoglobin is a monomer. Both hemoglobin and myoglobin contain a prosthetic group called heme, which contains a central iron atom.arrow_forward
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