Department of Chemistry and Biochemistry, University of California, San Diego, USA
Review
Equation of State for O2-Binding by Hemoglobin in Human Red Blood Cells
Author(s): Francis Knowles* and Douglas Magde
O2-Equilibrium binding data of hemoglobin in whole blood under standard conditions was fitted to an equation of state comprised of three unknown quantities: Kα, the equilibrium constant for binding O2 by equivalent low affinity α-chains; KΔ, a dimensionless equilibrium constant describing the change between low-and high-affinity structures of hemoglobin, Tstate and Rstate; Kβ, the equilibrium constant for binding O2 by equivalent high affinity β-chains. Values of the unknown quantities at pH 7.4 and 37°C are: Kα=15,090 L/mol; KΔ=0.0260; Kβ=393,900 L/mol. A graph of predicted versus observed values of fractional saturation, F, is linear: FPRE=0.9998 FOBS=0.0005, R2=0.9997. The Perutz/Ad.. View more»