Haemoglobin

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  • Created by: emma
  • Created on: 05-03-14 21:33
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  • Haemoglobin
    • Exercise
      • Tissues respire quickly which uses up the surrounding O2
        • ppO2 lower than normal so the Hb has less affinity for O2
          • More O2 unloaded to tissues for respiration
    • Loading and Unloading
      • Loading (O2 is taken up by haemoglobin)
        • At high ppO2 more O2 is loaded
      • Unloading (O2 is released)
        • At low ppO2 oxygen is unloaded
    • Partial pressure
      • At high ppO2  (in lungs) Haemoglobin has a high affinity for O2
        • Hb becomes fully saturated
      • At low ppO2 (in tissue) Hb has a low affinity for O2
        • O2 is unloaded to surrounding tissues
    • Structure
      • Large protein
      • Quaternary structure
        • 4 sub units with 4 haem groups
          • Can hold up to 4 O2 molecules
    • Bohr shift
      • At high CO2 levels Hb's affinity for O2 is lowered
        • CO2 levels increase and saturation of Hb decreases
          • Caused by increased levels of CO2
          • More O2 unloaded to respiring tissues
      • O2 dissociation curve shifts to right
      • CO2 makes the blood acidic
        • Alter in PH changes tertiary structure of  Hb
    • Different organisms
      • Animals living in environments with little O2
        • Hb has a higher affinity for O2
          • Hb becomes more saturated at lower levels of O2
      • Animals with a high metabolic rate
        • Hb has a lower affinity for O2
          • O2 dissociates from Hb more readily to supply tissues with O2

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