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The oxygen–hemoglobin dissociation curve, also called the oxyhemoglobin dissociation curve or oxygen dissociation curve (ODC), is a curve that plots the proportion of hemoglobin in its saturated (oxygen-laden) form on the vertical axis against the prevailing oxygen tension on the horizontal axis. This curve is an important tool for ...
Hemoglobin's oxygen binding affinity (see oxygen–haemoglobin dissociation curve) is inversely related both to acidity and to the concentration of carbon dioxide. [1] That is, the Bohr effect refers to the shift in the oxygen dissociation curve caused by changes in the concentration of carbon dioxide or the pH of the environment.
Vice versa, it is true that a high concentration of CO 2 facilitates dissociation of oxyhemoglobin, though this is the result of two distinct processes (Bohr effect and Margaria-Green effect) and should be distinguished from Haldane effect.
The shift encourages oxygen to bind to the three remaining heme units within hemoglobin (thus, oxygen binding is cooperative). [citation needed] Classically, the iron in oxyhemoglobin is seen as existing in the iron(II) oxidation state.
2,3-BPG may also serve to physiologically counteract certain metabolic disturbances to the oxygen-hemoglobin dissociation curve. For example, at high altitudes , low atmospheric oxygen content of oxygen can cause hyperventilation and resultant metabolic alkalosis which causes an abnormal left-shift of the oxygen-hemoglobin dissociation curve ...
After the human body reaches around 2,100 metres (6,900 ft) above sea level, the saturation of oxyhemoglobin begins to decrease rapidly. [2] However, the human body has both short-term and long-term adaptations to altitude that allow it to partially compensate for the lack of oxygen.
Its oxygen-hemoglobin dissociation curve is shifted to the left, meaning that it is able to absorb oxygen at lower concentrations than adult hemoglobin. This enables fetal hemoglobin to absorb oxygen from adult hemoglobin in the placenta, where the oxygen pressure is lower than at the lungs.
The Root effect is a physiological phenomenon that occurs in fish hemoglobin, named after its discoverer R. W. Root.It is the phenomenon where an increased proton or carbon dioxide concentration (lower pH) lowers hemoglobin's affinity and carrying capacity for oxygen.