Haemoglobin
- Created by: helenoodle
- Created on: 12-11-13 10:40
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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
- Lower affinity
- Left shift
- Higher affinity
- Efficient to intake O2
- Higher affinity
- Foetus have move affinity
- otherwise haemoglobin would diffuse into mother instead
- Right shift (Bohr)
- Lungs
- High affinity
- Higher partial pressure
- Efficient intake of oxygen
- more o2
- Efficient intake of oxygen
- Higher partial pressure
- High affinity
- Tissues
- Low affinity
- Lower partial pressure
- Efficient offload of oxygen (dissociate)
- less o2
- Efficient offload of oxygen (dissociate)
- Lower partial pressure
- Low affinity
- Quaternary structure
- 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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