1.5% of inhaled O2 dissolves in the blood plasma, while 98.5% of inhaled O2 bind to haemoglobin in the red blood cells. |
Heme portion of haemoglobin contains 4 iron atoms, each of which binds to an oxygen molecule. |
Oxygen and haemoglobin combine in a reversible reaction to form oxyhemoglobin. |
Relationship between Oxyhemoglobin and Partial Pressure of Oxygen: |
The higher the PO2, the more oxygen will bind to haemoglobin. When reduced haemoglobin is completely converted into oxyhemoglobin, it is said to be fully saturated. When haemoglobin is a mix of Hb and Hb-O2, it is said to be partially saturated. |
Percent Saturation of Haemoglobin: average saturation of haemoglobin with oxygen. |
The relation between the Percent Saturation and Partial Pressure of Oxygen is illustrated by Oxygen- Haemoglobin Dissociation Curve. |
When PO2=20 (deoxygenated blood in contracting skeletal muscles), percent saturation = 35% |
When PO2=40 (deoxygenated blood in systemic veins), percent situation = 75% |
When PO2=100 (oxygenated blood in systemic arteries), percent saturation is near 100. |
Factors Influencing Affinity of Haemoglobin towards Oxygen: |
1. Acidity: An increase in acidity, causes affinity of haemoglobin to O2 to decrease. Hence, curve shifts right. Decreases affinity means oxygen more readily dissociates from the haemoglobin and is more easily available to tissue cells. |
#Bohr's Effect: the effect of pH on the affinity of haemoglobin towards oxygen. An increase in H+ in blood causes O2 to unload from haemoglobin and the binding of haemoglobin to oxygen causes unloading of H+ from haemoglobin. The explanation for the Bohr effect is that hemo- globin can act as a buffer for hydrogen ions (H). But when H ions bind to amino acids in haemoglobin, they alter its structure slightly, decreasing its oxygen-carrying capacity. |
2. Partial Pressure of CO2: As CO2 enters the blood, much of it is converted into carbonic acid (H2CO3), a reaction catalysed by and enzyme in RBC called carbonic anhydrase. The carbonic acid does formed dissociates into bicarbonate ions and H+ ions. As H+ ion concentration in blood increases, acidity increases, causing more dissociation of oxygen from haemoglobin. Dissociation curve moves right. |
3. Temperature: Within limits, an increase in temperature promotes unloading of O2 from haemoglobin. Metabolically active cells release acids and heat which in turn promote release of O2 from haemoglobin to be used by them. |
4. 2,3-bisphosphoglycerate: decreases affinity of haemoglobin towards oxygen. Certain hormones such as hGH, thyroxine epinephrine, norepinephrine and testosterone increase BPG production. , |
Foetal Haemoglobin has a much greater affinity to oxygen that adult haemoglobin. This is very important because the O2 saturation in maternal blood in the placenta is quite low, and the foetus might suffer hypoxia were it not for the greater affinity of foetal haemoglobin for O2.
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