Video narration
The oxyhaemoglobin dissociation curve shows the relationship between the partial pressure of oxygen and the percentage saturation of haemoglobin with oxygen. First, draw the axes. The horizontal X-axis represents the partial pressure of oxygen, or PaO₂, in kilopascals. The vertical Y-axis represents haemoglobin oxygen saturation, in percent. The curve is sigmoid, or S-shaped, because haemoglobin exhibits cooperative binding: when one oxygen molecule binds, haemoglobin becomes more likely to bind the next. Now, remember three important points. The arterial point is approximately 13.3 kilopascals, with haemoglobin saturation around 97 to 98 percent. The mixed venous point is approximately 5.3 kilopascals, with saturation around 75 percent. P-fifty is the partial pressure of oxygen at which haemoglobin is 50 percent saturated. Its normal value is approximately 3.5 kilopascals, or 26 to 27 millimetres of mercury. What does the shape tell us? The flat upper portion means that haemoglobin saturation changes relatively little despite moderate falls in oxygen partial pressure. This provides a safety margin for oxygen loading in the lungs. The steep lower portion means that a small fall in oxygen partial pressure can produce substantial oxygen unloading in the tissues. Now, understand shifts of the curve. A right shift means reduced haemoglobin affinity for oxygen. P-fifty increases, so haemoglobin releases oxygen more readily to the tissues. Remember: increased carbon dioxide, increased hydrogen ion concentration or decreased pH, increased temperature, and increased 2,3-DPG cause a right shift. Use the mnemonic CADET, face Right: Carbon dioxide, Acid, 2,3-DPG, Exercise, and Temperature. A left shift means increased haemoglobin affinity for oxygen. P-fifty decreases, so haemoglobin holds onto oxygen more tightly, which can reduce tissue unloading. Causes include decreased carbon dioxide, increased pH, decreased temperature, decreased 2,3-DPG, and fetal haemoglobin. Carbon monoxide and methaemoglobin also shift the remaining oxygen-binding sites to the left.