- Oxygen-haemoglobin dissociation curve
The oxygen-haemoglobin dissociation curve plots the proportion of
hemoglobinin its saturated form on the vertical axis against the prevailing oxygentension on the horizontal axis. The oxyhemoglobin dissociation curve is an important tool for understanding how our blood carries and releases oxygen. Specifically, the oxyhemoglobin dissociation curve relates oxygen saturation (SO2) and partial pressure of oxygen in the blood (PO2), and is determined by what is called "hemoglobin's affinity for oxygen"; that is, how readily hemoglobin acquires and releases oxygen molecules into the fluid that surrounds it.
Hemoglobin (Hb), a globular protein, is the primary vehicle for transporting oxygen in the blood. Oxygen is also carried dissolved in the blood's plasma, but to a much lesser degree. Hemoglobin is contained in erythrocytes, more commonly referred to as red blood cells.Under certain conditions, oxygen bound to the hemoglobin is released into the blood's plasma from where , and under other circumstances it is absorbed from the tissue into the blood. Each hemoglobin molecule has a limited capacity for holding oxygen molecules. How much of that capacity that is filled by oxygen bound to the hemoglobin at any time is called the oxygen saturation. Expressed as a percentage, the oxygen saturation is the ratio of the amount of oxygen bound to the hemoglobin, to the oxygen carrying capacity of the hemoglobin. The oxygen carrying capacity is determined by the amount of hemoglobin present in the blood.The amount of oxygen bound to the hemoglobin at any time is related, in large part, to the partial pressure of oxygen to which the hemoglobin is exposed. In the lungs, at the alveolar-capillary interface, the partial pressure of oxygen is typically high, and therefore the oxygen binds readily to hemoglobin that is present. As the blood circulates to other body tissue in which the partial pressure of oxygen is less, the hemoglobin releases the oxygen into the tissue because the hemoglobin cannot maintain its full bound capacity of oxygen in the presence of lower oxygen partial pressures.
It is usually a sigmoid plot. A hemoglobin molecule can bind up to four oxygen molecules in a reversible way.
The shape of the curve results from the interaction of bound oxygen molecules with incoming molecules. The binding of the first molecule is difficult. However, this facilitates the binding of the second and third molecules, and it is only when the fourth molecule is to be bound that the difficulty increases, partly as a result of crowding of the hemoglobin molecule, partly as a natural tendency of oxygen to dissociate.
In its basic form, the oxyhemoglobin dissociation curve describes the relation between the partial pressure of oxygen (x axis) and the oxygen saturation (y axis). Hemoglobin's affinity for oxygen increases as successive molecules of oxygen bind. More molecules bind as the oxygen partial pressure increases until the maximum amount that can be bound is reached. As this limit is approached, very little additional binding occurs and the curve levels out as the hemoglobin becomes saturated with oxygen. Hence the curve has a sigmoidal or S-shape. At pressures above about 60 mmHg, the standard dissociation curve is relatively flat, which means that the oxygen content of the blood does not change significantly even with large increases in the oxygen partial pressure. To get more oxygen to the tissue would require blood transfusions to increase the hemoglobin count (and hence the oxygen carrying capacity), or supplemental oxygen that would increase the oxygen dissolved in plasma.Although binding of oxygen to hemoglobin continues to some extent for pressures below about 60 mmHg, as oxygen partial pressures decrease in this steep area of the curve, the oxygen is unloaded to peripheral tissue readily as the hemoglobin's affinity diminishes.The partial pressure of oxygen in the blood at which the hemoglobin is 50% saturated, typically about 26.6 mmHg for a healthy person, is known as the P50. The P50 is a conventional measure of hemoglobin affinity for oxygen. In the presence of disease or other conditions that change the hemoglobin's oxygen affinity and, consequently, shift the curve to the right or left, the P50 changes accordingly. An increased P50 indicates a rightward shift of the standard curve, which means that a larger partial pressure is necessary to maintain a 50% oxygen saturation. This indicates a decreased affinity. Conversely, a lower P50 indicates a leftward shift and a higher affinity.
The 'plateau' portion of the oxyhemoglobin dissociation curve is the range that exists at the pulmonary capillaries (minimal reduction of oxygen transported until the p(O2) falls below 60 mmHg).
The 'steep' portion of the oxyhemoglobin dissociation curve is the range that exists at the systemic capillaries (a small drop in systemic capillary p(O2) can result in the release of large amounts of oxygen for the metabolically active cells).
To see the relative affinities of each successive oxygen as you remove/add oxygens from/to the haemoglobin from the curve compare the relative increase/decrease in p(O2) needed for the corresponding increase/decrease in s(O2).
Factors shifting curve
Many factors influence the affinity of this binding and alter the shape of the curve:
Left shift of the curve is a sign of hemoglobin's increased affinity for oxygen (eg. at the lungs). Similarly, right shift shows decreased affinity, as would appear with an increase in body temperature, hydrogen ion,
2,3-bisphosphoglycerate(also known as diphosphoglycerate) or carbon dioxide concentration (the Bohr effect) Carbon monoxidehas a much higher affinity for haemoglobin than oxygen does. In carbon monoxide poisoning, oxygen cannot be transported and released to body tissues thus resulting in hypoxia.
With fetal hemoglobin, the shift facilitates diffusion of oxygen across the
placenta. The oxygen dissociation curve for myoglobinexists even further to the left.
Factors that Affect the Standard Dissociation Curve
The strength with which oxygen binds to hemoglobin is affected by several factors. In effect these factors shift or reshape the oxyhemoglobin curve ("the standard curve"). The standard curve is shifted to the right by an increase in temperature, 2,3-BPG, or PCO2, or a decrease in pH.
A rightward shift indicates that the hemoglobin under study has a decreased affinity for oxygen. This makes it more difficult for hemoglobin to bind to oxygen (requiring a higher partial pressure of oxygen to achieve the same oxygen saturation), but it makes it easier for the hemoglobin to release oxygen bound to it. The effect of this rightward shift of the curve increases the partial pressure of oxygen in the tissues when it is most needed, such as during exercise, or hemorrhagic shock.
In contrast, the curve is shifted to the left by the opposite of these conditions. This leftward shift indicates that the hemoglobin under study has an increased affinity for oxygen so that hemoglobin binds oxygen more easily, but unloads it more reluctantly.
Variation of the hydrogen ion concentration
This changes the blood's pH. A decrease in pH shifts the standard curve to the right, while an increase shifts it to the left. This is known as the Bohr effect.
Effects of carbon dioxide
Carbon dioxide affects the curve in two ways: first, it influences intracellular pH (the Bohr effect), and second, CO2 accumulation causes carbamino compounds to be generated through chemical interactions. Low levels of carbamino compounds have the effect of shifting the curve to the right, while higher levels cause a leftward shift.
Effects of 2,3-DPG
2,3-Disphosphoglycerate (also 2,3 Bisphosphoglycerate or BPG), or 2,3-DPG, is an organophosphate, which is created in erythrocytes during glycolysis. The production of 2,3-DPG is likely an important adaptive mechanism, because the production increases for several conditions in the presence of diminished peripheral tissue O2 availability, such as hypoxemia, chronic lung disease, anemia, and congestive heart failure, among others. High levels of 2,3-DPG shift the curve to the right, while low levels of 2,3-DPG cause a leftward shift, seen in states such as septic shock and hypophosphatemia.
Temperature does not have so dramatic effect as the previous factors, but hyperthermia causes a rightward shift, while hypothermia causes a leftward shift.
Hemoglobin binds with carbon monoxide 240 times more readily than with oxygen. The presence of carbon monoxide on one of the 4 heme sites causes the oxygen on the other heme sites to bind with greater affinity. This makes it difficult for the hemoglobin to release the oxygen to the tissues and has the effect of shifting the curve to the left. With an increased level of carbon monoxide, a person can suffer from severe hypoxemia while maintaining a normal PO2.
Effects of Methemoglobinemia
Methemoglobinemiais a form of abnormal haemoglobin and causes a leftward shift in the curve.
Fetal hemoglobin (HbF) is structurally different from normal hemoglobin (Hb). The fetal dissociation curve is shifted to the left relative to the curve for the normal adult. Typically, fetal arterial oxygen pressures are low, and hence the leftward shift enhances the placental uptake of oxygen.At the placenta there is a higher concentration of 2,3-DPG formed. This binds more readily to adult hemoglobin but not to fetal heamoglobin. This causes the adult Hb to release more oxygen at the placenta to be taken up by the fetus. Fetal Hb is made up of gamma chains not beta ones, and 2,3-DPG does not bind readily to gamma chains, hence it does not give up its oxygen.
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