Architecture of Allosteric Structure. Equation of State Containing Three Unknown Quantities for Fractional Saturation of whole Human Blood with O2: Formatting the Adair Equation to Accommodate Ordered Equivalent Sequences of O2-Binding Reactions and a Single Conformation Change Not Concerted with O2 Binding

<p>O₂-Equilibrium binding data of hemoglobin in whole blood under standard conditions (Kernohan JC. & Roughton FJW (1972) in Oxygen Affinity of Hemoglobin and Red Cell Acid Base Status, ed Rorth and Astrup, Copenhagen, Munksgaard, pp 65-72; Severinghaus JW in <i>ibid</i> pp. xx-xx) was fitted to an equation of state comprised of three unknown quantities: <i>K</i>α, the equilibrium constant for binding O₂ by equivalent low affinity α-chains;<i> K_ΔC</i>, a dimensionless equilibrium constant describing the conformation change between low- and high-affinity conformations of hemoglobin, ^Tstate and ^Rstate; <i>K</i>_β, the equilibrium constant for binding O₂ by equivalent high affinity β-chains, the Perutz/Adair Equation. Values of the unknown quantities at pH 7.4 and 37^oC are: <i>K</i>_α= 15,090 L/mol; <i>K_ΔC</i> = 0.0260; <i>K</i>_β = 393,900 L/mol. </p> <p> </p> <p>A graph of predicted <i>versus</i> observed values of fractional saturation, <i>F</i>, is linear: <i>F</i>_PRE = 0.9998 <i>F</i>_OBS – 0.0005, r² =0.9997. The Perutz/Adair equation of state is defined as such insofar as all aspects of the stereochemical model (Perutz MF (1970) Nature London 228, 726-739) are imposed on the earlier sequential binding model of Adair (1925) JBC 63, 493-545.</p> <br>

Architecture of Allosteric Structure. Equation of State Containing Three Unknown Quantities for Fractional Saturation of whole Human Blood with O2: Formatting the Adair Equation to Accommodate Ordered Equivalent Sequences of O2-Binding Reactions and a Single Conformation Change Not Concerted with O2 Binding

<p>O₂-Equilibrium binding data of hemoglobin in whole blood under standard conditions (Kernohan JC. & Roughton FJW (1972) in Oxygen Affinity of Hemoglobin and Red Cell Acid Base Status, ed Rorth and Astrup, Copenhagen, Munksgaard, pp 65-72; Severinghaus JW in <i>ibid</i> pp. xx-xx) was fitted to an equation of state comprised of three unknown quantities: <i>K</i>α, the equilibrium constant for binding O₂ by equivalent low affinity α-chains;<i> K_ΔC</i>, a dimensionless equilibrium constant describing the conformation change between low- and high-affinity conformations of hemoglobin, ^Tstate and ^Rstate; <i>K</i>_β, the equilibrium constant for binding O₂ by equivalent high affinity β-chains, the Perutz/Adair Equation. Values of the unknown quantities at pH 7.4 and 37^oC are: <i>K</i>_α= 15,090 L/mol; <i>K_ΔC</i> = 0.0260; <i>K</i>_β = 393,900 L/mol. </p> <p> </p> <p>A graph of predicted <i>versus</i> observed values of fractional saturation, <i>F</i>, is linear: <i>F</i>_PRE = 0.9998 <i>F</i>_OBS – 0.0005, r² =0.9997. The Perutz/Adair equation of state is defined as such insofar as all aspects of the stereochemical model (Perutz MF (1970) Nature London 228, 726-739) are imposed on the earlier sequential binding model of Adair (1925) JBC 63, 493-545.</p> <br>