Questions and Answers
Which of the following is NOT a function of hemoglobin?
Defense against pathogens
What is the role of hemoglobin in the delivery of oxygen?
To transport oxygen to tissues
What is the effect of carbon monoxide on hemoglobin function?
It inhibits the binding of oxygen to hemoglobin
Which of the following is a negative allosteric effector of oxygen binding regulatory mechanisms in red cells?
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Which of the following hemoglobinopathies is caused by a point mutation in the adult β-globin gene?
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What is the effect of deoxygenation on the polymer formation of HbS?
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What is the preferred clinical index for diagnosing diabetes?
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Which of the following is a characteristic of myoglobin?
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Which of the following is true about the T and R states of hemoglobin?
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What is the major form of hemoglobin during fetal development?
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What effect does low pH or high CO2 have on the oxygen binding curve of hemoglobin?
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Which of the following is true about the structure of myoglobin?
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Which of the following is true about hemoglobin function?
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What is the major form of hemoglobin shortly after birth through adulthood?
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What is the effect of 2,3-bisphosphoglycerate (2,3-BPG or DPG) on oxygen binding?
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What effect does low pH or high CO2 have on the oxygen binding curve of hemoglobin?
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What is the difference between the T and R states of hemoglobin?
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What is the effect of carbon monoxide (CO) on hemoglobin function?
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What is the function of myoglobin during exercise?
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Which of the following is true about globin gene switching?
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What is the preferred clinical index for diagnosing diabetes?
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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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