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This is on as a "work in progress" - it's a bit (a bit?!?!?!) ugly at the moment but I'll tidy it up later - honest To fully understand these notes (if that is at all possible given the quality of them) you will need a diagram of an oxygen dissociation curves. A useful pdf document is available at www.curriculumpress.demon.co.uk/pdf/bio/09 oxygen curves.pdf 4 oxygen bind to 1 haemoglobin oxyhaemoglobin (oxygen to tissues) haemoglobin can bind to carbon dioxide carboxyhaemoglobin (carbon dioxide to lungs) at high oxygen conc (e.g. in lungs) almost all HB is oxyHb at middle oxygen conc (e.g. in vein between lung and heart, and arteries between heart and tissues) still almost all oxyHb at low oxygen conc (respiring tissues) oxygen dissociates Why is curve S-shaped not straight line? Each binding of an oxygen causes conformational change in Hb making next one bind more readily except the last one which does not bind oxygen very readily Bohr Effect carbon dioxide causes oxygen to dissociate more readily shifts curve to right Bohr effect is explained by chloride shift
Other curves foetal Hb has greater affinity than maternal (curve to left) myoglobin (pigment in muscle) has more affinity than Hb (curve to left) so retains oxygen until very low partial pressures - acts as an oxygen store for very strenuous exercise llama shows left show so more oxygen loading at low partial pressures increasing temperature reduces affinity (curve to right) this means that at active tissues (high temp) Hb unloads |