In acidosis and hyperthermia, the affinity of hemoglobin for oxygen is most likely to:

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Multiple Choice

In acidosis and hyperthermia, the affinity of hemoglobin for oxygen is most likely to:

In acidosis and hyperthermia, hemoglobin’s affinity for oxygen decreases and the oxygen dissociation curve shifts to the right. This is driven by the Bohr effect, where lower pH (more H+) and higher CO2 promote a form of hemoglobin that releases O2 more readily. Higher temperature further destabilizes the Hb–O2 bond. A rightward shift corresponds to an increased p50, meaning hemoglobin holds onto oxygen less tightly and unloads more to tissues. Clinically, this helps tissues receive more oxygen when they’re actively metabolizing or under stress. So the best description is decreased affinity with a rightward shift.

In acidosis and hyperthermia, hemoglobin’s affinity for oxygen decreases and the oxygen dissociation curve shifts to the right. This is driven by the Bohr effect, where lower pH (more H+) and higher CO2 promote a form of hemoglobin that releases O2 more readily. Higher temperature further destabilizes the Hb–O2 bond. A rightward shift corresponds to an increased p50, meaning hemoglobin holds onto oxygen less tightly and unloads more to tissues. Clinically, this helps tissues receive more oxygen when they’re actively metabolizing or under stress. So the best description is decreased affinity with a rightward shift.

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