Haemoglobin
- 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
- ppO2 lower than normal so the Hb has less affinity for O2
- Tissues respire quickly which uses up the surrounding O2
- 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
- Loading (O2 is taken up by haemoglobin)
- 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
- At high ppO2 (in lungs) Haemoglobin has a high affinity for O2
- Structure
- Large protein
- Quaternary structure
- 4 sub units with 4 haem groups
- Can hold up to 4 O2 molecules
- 4 sub units with 4 haem groups
- 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
- CO2 levels increase and saturation of Hb decreases
- O2 dissociation curve shifts to right
- CO2 makes the blood acidic
- Alter in PH changes tertiary structure of Hb
- At high CO2 levels Hb's affinity for O2 is lowered
- 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
- Hb has a higher affinity for 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
- Hb has a lower affinity for O2
- Animals living in environments with little O2
- Exercise
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