Hemoglobin P50 from the Dissociation Curve

Standard pH / T / pCO₂. Measure saturation S at several pO₂ and recover P50 from a Hill linearization: ln(S/(1−S)) versus ln pO₂.

University / research· 22 min·Related simulator: Biophysics, Fluids & GeoscienceOxygen-Hemoglobin Dissociation Curve

Goal

Determine P50 from S = pO₂ⁿ / (P50ⁿ + pO₂ⁿ). A plot of ln(S/(1−S)) versus ln pO₂ has intercept −n ln P50, so P50 = exp(−intercept / slope).

Equipment

  • Blood tonometer
  • Oximeter
  • pO₂ control
  • Standard pH / T / pCO₂

Experiment

Theory

The Hill plot is linear in log–log coordinates. The bench hides effective P50, n and any “right/left shift” label. Conditions are standard (pH 7.40, 37 °C, pCO₂ 40 mmHg) so you recover the usual adult P50.

Procedure

  1. pH, temperature and pCO₂ are fixed at standard values. P50 is hidden. You only change pO₂.
  2. Record the oximeter saturation S (as a fraction). Small noise is added. There is no live P50.
  3. The notebook computes ln(S/(1−S)) and ln pO₂. Use points with S roughly between 0.15 and 0.85.
  4. Repeat for at least 6 oxygen tensions from about 12 to 70 mmHg.
  5. Fit the Hill plot; P50 = exp(−intercept / slope). Compare with the reference.

Conclusion

The fitted P50 agrees with the hidden standard adult value. Main uncertainties: oximeter noise and the Hill-equation idealization.