Haemoglobin Flashcards

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1
Q

What is the structure of haemoglobin?

A
  • 4 polypeptide chains
  • each polypeptide chain associated with a haem group
  • each haem group contains an iron ion in the centre which binds to oxygen
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2
Q

What does affinity mean?

A

The degree to which a substance tends to combine with another

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3
Q

Features of haemoglobin with a high affinity for oxygen

A

Will bind to oxygen easily but release less easily

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4
Q

Features of haemoglobin with a low affinity for oxygen

A

Will not bind to oxygen easily but will release it easily

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5
Q

What is partial pressure?

A

The amount of gas present in a mixture of gases is measured by its contribution to the total pressure of the gas mixture (kPa)

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6
Q

Explain how haemoglobin associates with oxygen in the lungs

A
  • High partial pressure of O2
  • O2 gets pressed onto haemoglobin molecules in RBCs so association occurs
  • Haemoglobin leaves lungs fully saturated
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7
Q

Explain how haemoglobin dissociates with oxygen in respiring cells

A
  • Low partial pressure of O2
  • O2 dissociates from haemoglobin
  • Diffuses into respiring cells
  • Haemoglobin now unsaturated
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8
Q

Define cooperative binding

A

Binding of one molecule affects the binding affinity of subsequent molecules

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9
Q

Factors affecting oxygen dissociation curve

A
  • The organism’s environment (O2 availability)
  • How metabolically active the organism is
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10
Q

If the oxygen dissociation curve is shifted left does the haemoglobin have a higher or lower affinity for oxygen?

A

Higher

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11
Q

Which way would the oxygen dissociation curve shift for a metabolically active organism?

A

Right - lower affinity in order to supply sufficient oxygen

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12
Q

What is The Bohr Effect?

A

Carbon dioxide reduces haemoglobin’s affinity for oxygen.

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13
Q

What 3 things cause the Bohr Effect?

A
  • High CO2 concentration
  • Low pH
  • High temperature
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