hard · MCAT bio-biochem
A laboratory researcher measures the oxygen affinity of adult hemoglobin (HbA) and fetal hemoglobin (HbF) in the presence of physiological concentrations of 2,3-BPG.
Which observation correctly explains the different O_2 binding behaviors?
- HbF has a right-shifted curve relative to HbA to ensure it can release O_2 to the fetal tissues.
- HbA has a higher affinity for O_2 because its β-chains are more receptive to 2,3-BPG than the γ-chains of HbF.
- Both show identical sigmoidal curves when 2,3-BPG is removed from the solution.
- HbF has a higher affinity for O_2 because it binds 2,3-BPG less effectively than HbA.
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