O2 dissociation curve is shifted to right in all except?
Now, the correct answer is the one that doesn't fit here. Let me think about possible distractors. Common options might include things like alkalosis, which would shift the curve left. Also, carbon monoxide poisoning shifts the curve left because CO binds to hemoglobin, reducing oxygen binding and causing a left shift. Similarly, fetal hemoglobin also has a left shift.
So if the options include something like "alkalosis" or "CO poisoning," those would be incorrect in the context of a right shift. The correct answer would be one of these. Let me check the standard list again. Right shift: high altitude (hypoxia), acidosis, hypercapnia, fever, increased 2,3-BPG. Left shift: hypothermia, alkalosis, hypoxia (in some contexts?), CO, fetal Hb.
Assuming the options are something like A. Acidosis, B. Hypercapnia, C. Alkalosis, D. Fever. Then the correct answer is C. Alkalosis. So the question is phrased as "all except," so the answer is the one that causes a left shift. Therefore, the correct answer is the option that is a left shifter. Let me confirm the mechanisms each factor has on the curve. Alkalosis (high pH) increases hemoglobin's affinity for oxygen, so the curve shifts left. So in the question, the correct answer is the one that does not cause a right shift, which would be alkalosis. So the answer is C. Alkalosis.
**Core Concept**
The oxygen dissociation curve describes hemoglobin's affinity for oxygen. A rightward shift indicates decreased affinity (promoting oxygen release), caused by acidosis, hypercapnia, increased temperature, or 2,3-BPG. A leftward shift increases affinity (reducing release), seen in alkalosis, hypothermia, or CO poisoning.
**Why the Correct Answer is Right**
Alkalosis (elevated pH) increases hemoglobin's oxygen affinity, shifting the curve left. This is due to the Bohr effect, where protonation of histidine residues in hemoglobin stabilizes the deoxy (T) state at lower pH. Conversely, alkalosis deprotonates these residues, favoring the oxy (R) state and reducing oxygen release.
**Why Each Wrong Option is Incorrect**
**Option A:** Hypercapnia (elevated CO2) causes a right shift via direct binding to hemoglobin and acidification (CO2 β carbonic acid).
**Option B:** Increased temperature (e.g., fever) destabilizes hemoglobin's T-state, promoting oxygen release.
**Option D:** 2,3-BPG binds to deoxyhemoglobin, reducing oxygen affinity and shifting the curve right.
**Clinical Pearl / High-Yield Fact**
Remember the "Shift Right" acronym: