Haemoglobin Flashcards
State the molecule that transports oxygen around the body
haemoglobin
Describe the quaternary structure of haemoglobin
four polypeptides each with a heam group (containing iron) attached
What is association/loading in relation to oxygen?
when oxygen binds to haemoglobin
What is dissociation/unloading in relation to oxygen?
when oxygen is released from haemoglobin
Explain what we mean by a ‘high affinity’ for oxygen
haemoglobin that takes up oxygen more readily but releases it less readily
Explain what we mean by a ‘low affinity’ for oxygen
haemoglobin that takes up oxygen less readily but releases it more readily
Explain why haemoglobin needs to change its affinity for oxygen
it must have a high affinity at the gas exchange surface and a low affinity at the respiring tissues
How does the presence of carbon dioxide cause the affinity of haemoglobin to for oxygen to decrease?
carbon dioxide causes the shape of the heamoglobin to change
Explain why haemoglobin from different animals has different affinities for oxygen
each species has a different amino acid sequence, therefore different tertiary and quaternary structure and so differrent oxygen binding properties