Biochemistry of Blood and Hemoglobin
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Questions and Answers

Which of the following is NOT a function of hemoglobin?

  • Defense against pathogens (correct)
  • Transport of ions and molecules
  • Storage of ions and molecules
  • Muscle contraction
  • What is the role of hemoglobin in the delivery of oxygen?

  • To store oxygen in the blood
  • To buffer pH levels in the blood
  • To transport oxygen to tissues (correct)
  • To remove waste from the blood
  • What is the effect of carbon monoxide on hemoglobin function?

  • It enhances the binding of oxygen to hemoglobin
  • It has no effect on the binding of oxygen to hemoglobin
  • It inhibits the binding of oxygen to hemoglobin (correct)
  • It converts hemoglobin into a different molecule
  • Which of the following is a negative allosteric effector of oxygen binding regulatory mechanisms in red cells?

    <p>2,3-bisphosphoglycerate (2,3-BPG)</p> Signup and view all the answers

    Which of the following hemoglobinopathies is caused by a point mutation in the adult β-globin gene?

    <p>Sickle Cell Anemia (HbS)</p> Signup and view all the answers

    What is the effect of deoxygenation on the polymer formation of HbS?

    <p>Increases the rate and extent of polymer formation</p> Signup and view all the answers

    What is the preferred clinical index for diagnosing diabetes?

    <p>Glycated hemoglobin (HbA1c)</p> Signup and view all the answers

    Which of the following is a characteristic of myoglobin?

    <p>It exhibits hyperbolic binding</p> Signup and view all the answers

    Which of the following is true about the T and R states of hemoglobin?

    <p>The R state has more interactions and is more rigid</p> Signup and view all the answers

    What is the major form of hemoglobin during fetal development?

    <p>HbF</p> Signup and view all the answers

    What effect does low pH or high CO2 have on the oxygen binding curve of hemoglobin?

    <p>Shifts the curve to the right</p> Signup and view all the answers

    Which of the following is true about the structure of myoglobin?

    <p>It has non-polar amino acids lining the interior</p> Signup and view all the answers

    Which of the following is true about hemoglobin function?

    <p>It transports oxygen from peripheral tissues to the lungs</p> Signup and view all the answers

    What is the major form of hemoglobin shortly after birth through adulthood?

    <p>HbA</p> Signup and view all the answers

    What is the effect of 2,3-bisphosphoglycerate (2,3-BPG or DPG) on oxygen binding?

    <p>It decreases the oxygen affinity of hemoglobin</p> Signup and view all the answers

    What effect does low pH or high CO2 have on the oxygen binding curve of hemoglobin?

    <p>Shifts the curve to the right</p> Signup and view all the answers

    What is the difference between the T and R states of hemoglobin?

    <p>R state involves breaking ion pairs between the dimer pair interface</p> Signup and view all the answers

    What is the effect of carbon monoxide (CO) on hemoglobin function?

    <p>It inhibits the binding of oxygen to hemoglobin</p> Signup and view all the answers

    What is the function of myoglobin during exercise?

    <p>It releases oxygen to maintain high activity levels</p> Signup and view all the answers

    Which of the following is true about globin gene switching?

    <p>It produces a variety of different hemoglobin tetramers throughout development</p> Signup and view all the answers

    What is the preferred clinical index for diagnosing diabetes?

    <p>Hemoglobin A1c (HbA1c)</p> Signup and view all the answers

    Study Notes

    Hemoglobin Function and Regulation

    • Hemoglobin's primary function is to deliver oxygen from lungs to body tissues.
    • It does not function in the storage of oxygen.

    Hemoglobin and Oxygen Binding

    • Hemoglobin binds to oxygen in the lungs and releases it in body tissues.
    • Oxygen binding is regulated by allosteric effectors such as 2,3-bisphosphoglycerate (2,3-BPG or DPG), which decreases oxygen binding affinity.
    • Low pH or high CO2 shifts the oxygen binding curve to the right, reducing oxygen binding affinity.
    • Carbon monoxide (CO) binds to hemoglobin with high affinity, reducing oxygen delivery.

    Hemoglobinopathies

    • Sickle cell anemia is a hemoglobinopathy caused by a point mutation in the adult β-globin gene.
    • Deoxygenation of HbS leads to polymer formation, causing sickling of red blood cells.

    Myoglobin

    • Myoglobin is a oxygen-binding protein found in muscles.
    • It releases oxygen during muscle contraction, facilitating oxygen delivery.

    Hemoglobin Structure and Development

    • Hemoglobin F (fetal hemoglobin) is the major form of hemoglobin during fetal development.
    • Hemoglobin A (adult hemoglobin) is the major form of hemoglobin shortly after birth through adulthood.
    • Hemoglobin structure changes during development through globin gene switching.

    Clinical Diagnostics

    • The preferred clinical index for diagnosing diabetes is not defined by hemoglobin or myoglobin.
    • Hemoglobin A1c (HbA1c) is often used to diagnose and monitor diabetes.

    Hemoglobin States

    • The T (tense) state of hemoglobin has low oxygen binding affinity, while the R (relaxed) state has high oxygen binding affinity.
    • The transition from T to R state allows for cooperative oxygen binding.

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    Description

    Test your knowledge of the biochemistry of blood and hemoglobin with this quiz. Learn about allosteric regulation, the role of hemoglobin in oxygen delivery, structural basis for cooperativity, and the effects of carbon monoxide.

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