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Related Experiment Videos

Oxygen binding constants for human hemoglobin tetramers.

S J Gill1, E Di Cera, M L Doyle

  • 1Department of Chemistry and Biochemistry, University of Colorado, Boulder 80309-0215.

Biochemistry
|June 30, 1987
PubMed
Summary

High-precision studies reveal an unexpectedly low contribution from triply ligated human hemoglobin (HbA0) species. This finding impacts understanding oxygen binding equilibrium constants.

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Area of Science:

  • Biochemistry
  • Physiological Chemistry

Background:

  • Hemoglobin (HbA0) is crucial for oxygen transport in the blood.
  • Understanding oxygen binding to hemoglobin is vital for physiological studies.
  • Previous studies have not fully resolved the contributions of intermediate ligated species.

Purpose of the Study:

  • To precisely quantify oxygen binding to human hemoglobin (HbA0) at near-physiological concentrations.
  • To investigate the contribution of the triply ligated species to oxygen binding.
  • To analyze binding reactions using overall Adair equilibrium constants.

Main Methods:

  • Differential oxygen-binding measurements using a thin-layer apparatus.
  • Studies conducted on human hemoglobin solutions at high concentrations (2-12 mM heme).

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  • Experiments performed at physiological pH ranges (7.0-9.1) in various buffers.

    • Main Results:

    • An unmeasurably low contribution from the triply ligated hemoglobin species was observed.
    • High HbA0 concentrations avoided tetramer dissociation into dimers, simplifying analysis.
    • The analysis utilized a tetramer-binding polynomial with overall Adair equilibrium constants.

    Conclusions:

    • The triply ligated species has a negligible impact on oxygen binding.
    • Equilibrium constants for the third and fourth stepwise oxygen binding reactions are practically undeterminable.
    • This finding necessitates a re-evaluation of current hemoglobin oxygen-binding models.