Haemoglobin Flashcards

1
Q

State the molecule that transports oxygen around the body

A

haemoglobin

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2
Q

Describe the quaternary structure of haemoglobin

A

four polypeptides each with a heam group (containing iron) attached

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3
Q

What is association/loading in relation to oxygen?

A

when oxygen binds to haemoglobin

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4
Q

What is dissociation/unloading in relation to oxygen?

A

when oxygen is released from haemoglobin

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5
Q

Explain what we mean by a ‘high affinity’ for oxygen

A

haemoglobin that takes up oxygen more readily but releases it less readily

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6
Q

Explain what we mean by a ‘low affinity’ for oxygen

A

haemoglobin that takes up oxygen less readily but releases it more readily

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7
Q

Explain why haemoglobin needs to change its affinity for oxygen

A

it must have a high affinity at the gas exchange surface and a low affinity at the respiring tissues

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8
Q

How does the presence of carbon dioxide cause the affinity of haemoglobin to for oxygen to decrease?

A

carbon dioxide causes the shape of the heamoglobin to change

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9
Q

Explain why haemoglobin from different animals has different affinities for oxygen

A

each species has a different amino acid sequence, therefore different tertiary and quaternary structure and so differrent oxygen binding properties

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