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Questions and Answers
What is the structure of hemoglobin composed of?
What is the structure of hemoglobin composed of?
What are the two forms of hemoglobin structure?
What are the two forms of hemoglobin structure?
What is the composition of the haem (heme) complex?
What is the composition of the haem (heme) complex?
What kind of interactions hold the oxygenated hemoglobin dimers together?
What kind of interactions hold the oxygenated hemoglobin dimers together?
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How many additional bonds can the haem Fe2+ form?
How many additional bonds can the haem Fe2+ form?
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Which molecule is formed by the linkage of four pyrrole rings through methylene bridges in haem synthesis?
Which molecule is formed by the linkage of four pyrrole rings through methylene bridges in haem synthesis?
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Where does the formation of δ-aminolevulinic acid occur in haem synthesis?
Where does the formation of δ-aminolevulinic acid occur in haem synthesis?
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What is the major site for haem synthesis in the body?
What is the major site for haem synthesis in the body?
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Which factor causes the oxygen dissociation curve to shift to the right, leading to a decrease in the affinity of hemoglobin for oxygen?
Which factor causes the oxygen dissociation curve to shift to the right, leading to a decrease in the affinity of hemoglobin for oxygen?
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What is the end product of haem degradation that is formed in the intestine?
What is the end product of haem degradation that is formed in the intestine?
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Study Notes
Hemoglobin Structure
- Hemoglobin is composed of four polypeptide chains (α, β, γ, and δ) and four haem (heme) groups.
- The two forms of hemoglobin structure are:
- T-state (tense state): deoxygenated form
- R-state (relaxed state): oxygenated form
Haem (Heme) Complex
- The haem complex is composed of a porphyrin ring with a central iron atom (Fe2+).
- The haem complex can bind to oxygen, carbon monoxide, and other ligands.
Oxygenated Hemoglobin
- Oxygenated hemoglobin dimers are held together by salt bridges, hydrogen bonds, and van der Waals interactions.
Haem Fe2+ Interactions
- The haem Fe2+ can form six additional bonds: one with oxygen, one with histidine, and four with the porphyrin ring.
Haem Synthesis
- The molecule formed by the linkage of four pyrrole rings through methylene bridges is protoporphyrin IX.
- The formation of δ-aminolevulinic acid occurs in the mitochondria.
- The major site for haem synthesis in the body is the liver and bone marrow.
Oxygen Dissociation Curve
- An increase in 2,3-bisphosphoglycerate (BPG) causes the oxygen dissociation curve to shift to the right, leading to a decrease in the affinity of hemoglobin for oxygen.
Haem Degradation
- The end product of haem degradation that is formed in the intestine is stercobilin, which is then excreted in the feces.
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Description
Test your knowledge about the inheritance patterns of ABO blood groups and the structure of hemoglobin. This quiz covers topics such as ABO blood group inheritance, types of RBC (red blood cell), exposure to different blood groups, and the structure of hemoglobin.
