Podcast
Questions and Answers
Which of the following is NOT a function of hemoglobin?
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?
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?
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?
Which of the following is a negative allosteric effector of oxygen binding regulatory mechanisms in red cells?
Which of the following hemoglobinopathies is caused by a point mutation in the adult β-globin gene?
Which of the following hemoglobinopathies is caused by a point mutation in the adult β-globin gene?
What is the effect of deoxygenation on the polymer formation of HbS?
What is the effect of deoxygenation on the polymer formation of HbS?
What is the preferred clinical index for diagnosing diabetes?
What is the preferred clinical index for diagnosing diabetes?
Which of the following is a characteristic of myoglobin?
Which of the following is a characteristic of myoglobin?
Which of the following is true about the T and R states of hemoglobin?
Which of the following is true about the T and R states of hemoglobin?
What is the major form of hemoglobin during fetal development?
What is the major form of hemoglobin during fetal development?
What effect does low pH or high CO2 have on the oxygen binding curve of hemoglobin?
What effect does low pH or high CO2 have on the oxygen binding curve of hemoglobin?
Which of the following is true about the structure of myoglobin?
Which of the following is true about the structure of myoglobin?
Which of the following is true about hemoglobin function?
Which of the following is true about hemoglobin function?
What is the major form of hemoglobin shortly after birth through adulthood?
What is the major form of hemoglobin shortly after birth through adulthood?
What is the effect of 2,3-bisphosphoglycerate (2,3-BPG or DPG) on oxygen binding?
What is the effect of 2,3-bisphosphoglycerate (2,3-BPG or DPG) on oxygen binding?
What effect does low pH or high CO2 have on the oxygen binding curve of hemoglobin?
What effect does low pH or high CO2 have on the oxygen binding curve of hemoglobin?
What is the difference between the T and R states of hemoglobin?
What is the difference between the T and R states of hemoglobin?
What is the effect of carbon monoxide (CO) on hemoglobin function?
What is the effect of carbon monoxide (CO) on hemoglobin function?
What is the function of myoglobin during exercise?
What is the function of myoglobin during exercise?
Which of the following is true about globin gene switching?
Which of the following is true about globin gene switching?
What is the preferred clinical index for diagnosing diabetes?
What is the preferred clinical index for diagnosing diabetes?
Flashcards
Hemoglobin function
Hemoglobin function
Hemoglobin is a protein that carries oxygen from the lungs to the tissues and carbon dioxide back to the lungs.
Hemoglobin and oxygen delivery
Hemoglobin and oxygen delivery
Hemoglobin transports oxygen to tissues.
Carbon monoxide and hemoglobin
Carbon monoxide and hemoglobin
Carbon monoxide blocks oxygen from binding to hemoglobin.
2,3-BPG effect
2,3-BPG effect
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Sickle Cell Anemia cause
Sickle Cell Anemia cause
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Deoxygenation and HbS
Deoxygenation and HbS
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HbA1c and diabetes
HbA1c and diabetes
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Myoglobin binding
Myoglobin binding
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Hemoglobin T and R states
Hemoglobin T and R states
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Fetal hemoglobin
Fetal hemoglobin
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Low pH/CO2 and hemoglobin
Low pH/CO2 and hemoglobin
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Myoglobin structure
Myoglobin structure
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Hemoglobin transport
Hemoglobin transport
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Hemoglobin A and adulthood
Hemoglobin A and adulthood
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2,3-BPG and oxygen affinity
2,3-BPG and oxygen affinity
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Low pH/high CO2 effect
Low pH/high CO2 effect
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Hemoglobin T and R states difference
Hemoglobin T and R states difference
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Carbon monoxide's effect
Carbon monoxide's effect
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Myoglobin function in exercise
Myoglobin function in exercise
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Globin gene switching
Globin gene switching
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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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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.
