Haemoglobin

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  • Haemoglobin
    • Quaternary structure
      • Polypeptide chains
      • 4 haeme groups
        • High affinity up to 3rd haeme group filled
        • Can bind with o2 molecules
    • In red blood cells
    • Dissociation curves
      • Right shift (Bohr)
        • Lower affinity
          • Efficient offload
        • More CO2 from respiration
          • reduces affinity
      • Left shift
        • Higher affinity
          • Efficient to intake O2
      • Foetus have move affinity
        • otherwise haemoglobin would diffuse into mother instead
    • Lungs
      • High affinity
        • Higher partial pressure
          • Efficient intake of oxygen
            • more o2
    • Tissues
      • Low affinity
        • Lower partial pressure
          • Efficient offload of oxygen (dissociate)
            • less o2
  • So: Affinity low = Bohr/Tissues (lower partial pressure) Efficient offload O2 More CO2
  • Affinity high = Lungs (steep/left shift) Efficient intake O2 Less CO2
  • More oxygen situations
    • Light (photosynthesis)
    • can dissolve in water (concentration higher)
    • More red blood cells
      • more haemogloblin = oxyhaemoglobin
    • More o2 = less co2

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