haemoglobin
- Created by: Margaret Hobart
- Created on: 13-05-21 16:44
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- Haemoglobin (Hb)
- found in red blood cells
- quaternary protein
- 4 polypeptide chains
- each coiled into a helix
- contains heam group which contains Fe2+
- 4 polypeptide chains
- transports O2
- each each can carry 4 O2 molecules
- O2 joins to Hb in RBC to form oxyhemoglobin
- reversible reaction
- Hb+4O2 ? HbO3
- Hb saturation depends on the particle pressure of O2 (pO2)
- pO2 measures O2 concentration - the higher the pO2 the greater the concentration of dissolved O2
- pCO2 is the CO2 concentrationin cells
- Hb gives up O2 at higher pCO2
- O2 loads into Hb to form HbO8 where there's a high pO2. Oxyheamaglobin unloads its O2 where there's a lower pO2
- O2 enters capillaries at the alveoli. alveoli have high pO2 so O2 loads onto Hb to form HbO8
- when cells respire pO2 lowers because RBCs deliver HbO8 to retiring tissues where it unloads O2
- the dissociation curve for adult human haemoglobin
- s-shape because when the Hb combines with the first O2 its shape alters in a way that makes it easier for others to join.
- as Hb becomes more saturated its harder for O2 molecules to join
- s-shape because when the Hb combines with the first O2 its shape alters in a way that makes it easier for others to join.
- adaptation
- organisms that live in low O2 concentrationenvironmentshave higher O2 affinity
- curve shifts left
- the dissociation curve for adult human haemoglobin
- s-shape because when the Hb combines with the first O2 its shape alters in a way that makes it easier for others to join.
- as Hb becomes more saturated its harder for O2 molecules to join
- s-shape because when the Hb combines with the first O2 its shape alters in a way that makes it easier for others to join.
- the dissociation curve for adult human haemoglobin
- curve shifts left
- organisms that live in low O2 concentrationenvironmentshave higher O2 affinity
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