Fitting abnormal oxygen equilibrium curves of hemoglobin.
A growing number of oxygen equilibrium curves for hemoglobin (Hb) mutants, post-translational modifications, or the binding of potent new effectors of Hb cannot be fitted adequately with the two-state model. Examples are curves showing double maxima in the derivative of the Hill plot, or slopes of less than unity. We present such examples of modified hemoglobins and strong effectors in this study and calculate at which substate level the two-state model differs from the data. Analysis of hemoglobin oxygen equilibrium curves is reconsidered using the two-state model extended to allow variation of the individual substate probabilities. In this way the effect on the equilibrium due to perturbations in energy of each substate can be studied as a diagnostic tool.
Marden
M C
MC
INSERM U299, Hôpital de Bicêtre, France.
Kister
J
J
Poyart
C
C
D000494:Allosteric Regulation; D000495:Allosteric Site; D001665:Binding Sites; D001731:Bisphosphoglycerate Mutase / Q000172:deficiency; D006441:Hemoglobin A / Q000378:metabolism*; D006455:Hemoglobins, Abnormal / Q000378:metabolism*; D006801:Humans; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D008024:Ligands; D046911:Macromolecular Substances; D008962:Models, Theoretical; D010108:Oxyhemoglobins / Q000378:metabolism*; D011336:Probability
D006455:Hemoglobins, Abnormal; D008024:Ligands; D046911:Macromolecular Substances; D010108:Oxyhemoglobins; D006441:Hemoglobin A; C029774:oxyhemoglobin A; D001731:Bisphosphoglycerate Mutase