Adair-based hemoglobin equilibrium with oxygen, carbon dioxide and hydrogen ion activity
| Autor: | Tomáš Kulhánek, Marek Mateják, Stanislav Matousek |
|---|---|
| Rok vydání: | 2015 |
| Předmět: |
Acid-Base Equilibrium
Binding Sites Hydrogen Clinical Biochemistry Temperature chemistry.chemical_element Oxygen–haemoglobin dissociation curve General Medicine Carbon Dioxide Oxygen Models Biological Hemoglobins Hemoglobin A chemistry Oxyhemoglobins Physical chemistry Humans Titration Hemoglobin Protons Oxygen binding |
| Zdroj: | Scandinavian journal of clinical and laboratory investigation. 75(2) |
| ISSN: | 1502-7686 |
| Popis: | As has been known for over a century, oxygen binding onto hemoglobin is influenced by the activity of hydrogen ions (H⁺), as well as the concentration of carbon dioxide (CO₂). As is also known, the binding of both CO₂and H⁺ on terminal valine-1 residues is competitive. One-parametric situations of these hemoglobin equilibria at specific levels of H⁺, O₂or CO₂are also well described. However, we think interpolating or extrapolating this knowledge into an 'empirical' function of three independent variables has not yet been completely satisfactory. We present a model that integrates three orthogonal views of hemoglobin oxygenation, titration, and carbamination at different temperatures. The model is based only on chemical principles, Adair's oxygenation steps and Van't Hoff equation of temperature dependences. Our model fits the measurements of the Haldane coefficient and CO₂hemoglobin saturation. It also fits the oxygen dissociation curve influenced by simultaneous changes in H⁺, CO₂and O₂, which makes it a strong candidate for integration into more complex models of blood acid-base with gas transport, where any combination of mentioned substances can appear. |
| Databáze: | OpenAIRE |
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