Haemoglobin Flashcards

1
Q

Where is haemoglobin found?

A

In red blood cells

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2
Q

What is the role of haemoglobin?

A

To carry oxygen around the body

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3
Q

What protein structure does haemoglobin have?

A

Quaternary

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4
Q

How many polypeptide chains make up haemoglobin?

A

4

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5
Q

What does each chain have?

A

A haem group containing an iron ion

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6
Q

How many oxygen molecules can haemoglobin carry?

A

4

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7
Q

What does haemoglobin become when oxygen binds to it?

A

Oxyhaemoglobin

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8
Q

What is association/loading?

A

When an oxygen molecule joins to the haemoglobin

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9
Q

What is dissociation/unloading?

A

When an oxygen molecule leaves oxyhaemoglobin

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10
Q

What does having an affinity for oxygen mean?

A

The tendency a molecule has to bind with oxygen

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11
Q

What affects haemoglobin’s affinity for oxygen?

A

Partial pressure of oxygen

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12
Q

The greater the concentration of dissolved oxygen in cells…

A

the higher the partial pressure

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13
Q

Does an increase or decrease in partial pressure cause an increase in haemoglobins affinity for oxygen?

A

Increase

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14
Q

When does oxygen load onto haemoglobin?

A

When theres a high partial pressure

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15
Q

When does oxyhaemoglobin unload oxygen?

A

When theres a lower partial pressure

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16
Q

Do alveoli have a high or low partial pressure? What does this mean happens to the oxygen?

A

High

It loads onto haemoglobin

17
Q

Does respiring tissue have a high or low partial pressure?

A

Low

18
Q

Does oxygen load or unload at respiring tissues?

A

Unload

19
Q

An increase in respiration in the tissue of a mammal affects the oxygen dissociation curve of haemoglobin. Describe and explain how. (2 marks)

A
  • Respiration produces CO2

- The curve will shift to the right (Bohr shift) so there will be more unloading

20
Q

Describe how the haemoglobin in one organisms may have a different chemical structure from the haemoglobin in another organism (1 mark)

A

Different number of polypeptide chains