oxygen dissociation curve

oxygen dissociation curve

1. transported by haemoglobin

   • primary structure: amino acids of 4 chains (a&b)
     • secondary structure: alpha helix
       • tertiary structure: loosely folded precisely for function
         • quaternary structure: globular 2alphaglobin and 2 betaglobin chains (4 polypeptides) with a haem group
   • readily accosiate with oxygen at exchange surface (alveoli)
     • readily dissociate at respiring tissues

2. oxygen affinity

   • cooperative binding
     • increases haemoglobins affinity as O2 is added which changes its shape.
   • in presence of CO2 o2 binding is more loose
     • good in respiring tissues

3. high affinity

   • low oxygen in area
     • high association and low dissociation
       • low metabolic rate
   • left

4. low affinity

   • high oxygen in area
     • low association and high dissociation
       • high metabolic rate
   • right