8418152
Description
oxygen dissociation curve
- 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
- quaternary structure: globular 2alphaglobin and 2 betaglobin chains (4 polypeptides) with a haem group
- tertiary structure: loosely folded precisely for function
- secondary structure: alpha helix
- readily accosiate with oxygen at exchange surface (alveoli)
- readily dissociate at respiring tissues
- readily dissociate at respiring tissues
- primary structure: amino acids of 4 chains (a&b)
- oxygen affinity
- cooperative binding
- increases haemoglobins affinity as O2 is added which changes its shape.
- increases haemoglobins affinity as O2 is added which changes its shape.
- in presence of CO2 o2 binding is more loose
- good in respiring tissues
- good in respiring tissues
- cooperative binding
- high affinity
- low oxygen in area
- high association and low dissociation
- low metabolic rate
- low metabolic rate
- high association and low dissociation
- left
- low oxygen in area
- low affinity
- high oxygen in area
- low association and high dissociation
- high metabolic rate
- high metabolic rate
- low association and high dissociation
- right
- high oxygen in area
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