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Questions and Answers
What is the molecular structure of fetal hemoglobin?
What is the molecular structure of fetal hemoglobin?
- [ζ₂γ₂] (2 zeta, 2 gamma)
- [ζ₂ε₂] (2 zeta, 2 epsilon)
- [α₂γ₂] (2 alpha, 2 gamma) (correct)
- [α₂β₂] (2 alpha, 2 beta)
Which type of hemoglobin is not present in adults?
Which type of hemoglobin is not present in adults?
- Gower I (correct)
- Gower II (correct)
- Portland (correct)
- Fetal Hgb (correct)
What proportion of fetal hemoglobin is typically found in newborns?
What proportion of fetal hemoglobin is typically found in newborns?
- 80% (correct)
- 40%
- 100%
- 60%
Which of the following hemoglobin forms has a molecular structure of [ζ₂γ₂]?
Which of the following hemoglobin forms has a molecular structure of [ζ₂γ₂]?
In which stage of life is Gower I hemoglobin found in significant proportions?
In which stage of life is Gower I hemoglobin found in significant proportions?
Flashcards
Portland Hemoglobin
Portland Hemoglobin
A type of hemoglobin with a molecular structure of [ζ₂γ₂] (2 zeta, 2 gamma), present only in newborns.
Gower I Hemoglobin
Gower I Hemoglobin
A type of hemoglobin with a molecular structure of [ζ₂ε₂] (2 zeta, 2 epsilon), present only at trace amounts in newborns.
Gower II Hemoglobin
Gower II Hemoglobin
A type of hemoglobin with a molecular structure of [α₂ε₂] (2 alpha, 2 epsilon), present only at trace amounts in newborns.
Fetal Hemoglobin
Fetal Hemoglobin
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Hemoglobin structure in newborns
Hemoglobin structure in newborns
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Hemoglobin structure in adults
Hemoglobin structure in adults
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Study Notes
Hemoglobin Forms
- Hemoglobin types vary depending on the stage of life and have different proportions in newborns and adults
- Portland: 2 zeta, 2 gamma (0% in newborns and adults)
- Gower I: 2 zeta, 2 epsilon (0% in newborns and adults)
- Gower II: 2 alpha, 2 epsilon (0% in newborns and adults)
- Fetal Hgb: 2 alpha, 2 gamma (80% in newborns and <1% in adults)
- A1/A: 2 alpha, 2 beta (20% in newborns and 97% in adults)
- A2: 2 alpha, 2 delta (<0.5% in newborns and 2.5% in adults)
Hemoglobin Derivatives
- Oxyhemoglobin (Hb O₂): Iron bound to oxygen, found in arterial blood (bright red) and is in the relaxed state
- Deoxygenated hemoglobin: Iron not bound to oxygen, found in venous blood (dark red), and it is in the tense state
- Carboxyhemoglobin (HbCO): Iron bound to carbon monoxide (CO), colorless gas, produced by humans. A poison that is silent. A killer, causes dizziness, nausea and exhaust from car - 240 times greater affinity to Hb than O2; cherry red color of blood and skin in CO poisoning
Dyshemoglobins
- Methemoglobin (Hi/Hemoglobin): Iron is in the ferric (Fe³⁺) state, can't bind to O₂, causes chocolate-brown color to blood.
- Sulfhemoglobin (SHb): Not measured by cyanmethaemoglobin method, mixture of oxidized, partially denatured Hb. Causes include prolonged constipation, bacteremia (C. perfringens), and enterogerous cyanosis; lavender-colored blood.
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