medium · 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.
Sign up free to see the explanation and track your rank →
More MCAT bio-biochem practice
- What genetic term describes a single gene influencing multiple seemingly unrelated traits?
- In the human ear, sound waves cause fluid in the cochlea to… — Which cells are responsible
- An electrophysiologist observes a neuron at its resting memb… — Which ion is primarily res
- Which structure is most likely dysfunctional?
- Which organelle would you expect to be exceptionally well-developed in these cells?
- Which molecule acts as a 'fluidity buffer' in animal cell membranes?
- A scientist is tracking the movement of a secreted protein. If the protein has just left t
- A molecule moves into a cell against its concentration gradient using energy provided by a