Concept explainers
(a) Interpretation:
Comparing the oxygen binding affinity of disulfide-bonded HbR and that of normal adult Hb (HbA).
Concept introduction:
In normal hemoglobin, the beta chain has the tyrosine residue at 145th position. The mutated hemoglobin named hemoglobin Rainier has cysteine in place of tyrosine. Another cysteine residue in the samesubunit forms a disulfide bond. This leads to conformational changes in the structureofhemoglobin.
(b) Interpretation:
The Bohr effect for disulfide bonded HbR as a reference to Bohr effect in HbA.
Concept introduction:
In normal hemoglobin, the beta chain has a tyrosine residue at 145th position. The mutated hemoglobin named hemoglobin Rainier has cysteine in place of tyrosine. Another cysteine residue in the same subunit forms a disulfide bond. This leads to conformational changes in the structure of hemoglobin.
(c) Interpretation:
The person that can adapt higher elevation more quickly and more slowly out of a person with disulfide-bonded HbR and a person with HbA.
Concept introduction:
In normal hemoglobin, the beta chain has a tyrosine residue at 145th position. The mutated hemoglobin named hemoglobin Rainier has cysteine in place of tyrosine. Another cysteine residue in the same subunit forms a disulfide bond. This leads to conformational changes in the structure of hemoglobin.
(d) Interpretation:
The person that can adapt higher elevation more quickly and more slowly out of a person with disulfide-bonded HbR and a person with HbA.
Concept introduction:
In normal hemoglobin, the beta chain has the tyrosine residue at 145th position. The mutated hemoglobin named hemoglobin Rainier has cysteine in place of tyrosine. Another cysteine residue in the same subunit forms a disulfide bond. This leads to conformational changes in the structure of hemoglobin.
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Biochemistry: Concepts and Connections (2nd Edition)
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