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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 ...
It was first conceptualized by August Krogh in 1919 with the help of Agner Krarup Erlang to describe oxygen supply in living tissues from human blood vessels. [1] [2] Its applicability has been extended to various academic fields, and has been successful explaining drug diffusion, water transport, and ice formation in tissues. [3]
The effect is also noted in the choroid rete, the network of blood vessels which carries oxygen to the retina. [3] In the absence of the Root effect, retia will result in the diffusion of some oxygen directly from the arterial blood to the venous blood, making such systems less effective for the concentration of oxygen. [ 4 ]
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.
The partial pressure of oxygen may be sufficient for example in anemia, but the hemoglobin content will be insufficient and subsequently as will be the oxygen content. Given enough supply of iron, vitamin B12 and folic acid , EPO can stimulate RBC production, and hemoglobin and oxygen content restored to normal.
A biological example of diffusion is the gas exchange that occurs during respiration within the human body. [7] Upon inhalation, oxygen is brought into the lungs and quickly diffuses across the membrane of alveoli and enters the circulatory system by diffusing across the membrane of the pulmonary capillaries. [8]
Fetal hemoglobin enhances the fetus' ability to draw oxygen from the placenta. This is facilitated by the hemoglobin molecule that made up of two alpha and two gamma chains (2α2γ). 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 ...
Venous oxygen saturation (SvO 2) is the percentage of oxygenated hemoglobin returning to the right side of the heart. It can be measured to see if oxygen delivery meets the tissues' demands. SvO 2 typically varies between 60% and 80%. [9] A lower value indicates that the body is in lack of oxygen, and ischemic diseases occur.