Mass Transport- Haemoglobin Flashcards

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1
Q

What contains haemoglobin?

A

Red blood cells

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2
Q

What is haemoglobin?

A

A large protein with a quaternary structure

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3
Q

What does each polypeptide chain have?

A

A haem group which contains an iron ion and gives haemoglobin its red colour

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4
Q

How many oxygen molecules can haemoglobin molecules carry?

A

4 so they have a high affinity for oxygen

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5
Q

What happens to haemoglobin in the lungs?

A

Joins with oxygen to become oxyhaemoglobin

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6
Q

What is the partial pressure of oxygen?

A

Measure of oxygen concentration

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7
Q

When is the partial pressure of oxygen higher?

A

When there is a greater concentration of dissolved oxygen in cells

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8
Q

What is the partial pressure of carbon dioxide?

A

Measure of the concentration of carbon dioxide in a cell

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9
Q

What determines how haemoglobin’s affinity for oxygen varies?

A

The partial pressure of oxygen

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10
Q

Where does oxygen load onto haemoglobin to form oxyhaemoglobin?

A

Where there’s a high partial pressure of oxygen

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11
Q

Where does oxyhaemoglobin unload its oxygen?

A

Where there’s a lower partial pressure of oxygen

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12
Q

Where does oxygen enter the lungs?

A

The blood capillaries at the alveoli that have a high partial pressure of oxygen so oxygen loads onto haemoglobin to form oxyhaemoglobin

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13
Q

What happens when cells respire?

A

They use up oxygen which lowers the partial pressure of oxygen- red blood cells deliver oxyhaemoglobin to respiring tissues where it unloads its oxygen, the haemoglobin then returns to the lungs to pick up more oxygen

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14
Q

What does the dissociation curve show?

A

How saturated the haemoglobin is with oxygen at any given partial pressure

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15
Q

What affinity does haemoglobin have at a high partial pressure of oxygen (in the lungs)?

A

High affinity- readily combine with oxygen so has a high saturation of oxygen

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16
Q

What affinity does haemoglobin have at a low partial pressure of oxygen (in respiring tissues)?

A

Low affinity- releases oxygen rather than combines with it so has a low saturation of oxygen

17
Q

Why is the dissociation curve ‘S-shaped?

A

When haemoglobin combines with the first oxygen molecule, its shape changes to make it easier for more oxygen molecules to join, but when haemoglobin becomes saturated it gets harder for oxygen molecules to join, curve has steep part in middle where it’s easier for oxygen molecules to join and shallow parts at ends where it’s harder

18
Q

How do partial pressures of carbon dioxide affect haemoglobin’s ability to give up oxygen?

A

Will give up oxygen more readily at higher partial pressures of carbon dioxide

19
Q

What is the Bohr effect?

A
  • When cells respire, produce carbon dioxide which raises the partial pressure of carbon dioxide
  • Increases rate of oxygen unloading so dissociation curve ‘shifts’ right, saturation of blood with oxygen is lower for a given partial pressure of oxygen so more oxygen is being released
20
Q

How is haemoglobin different in different organisms?

A
  • Organisms that live in environments with a low concentration of oxygen have haemoglobin with a higher affinity for oxygen than human haemoglobin- dissociation curve is to the left of ours
  • Organisms that are very active and have a high oxygen demand have haemoglobin with a lower affinity for oxygen than humans- dissociation curve is to the right of ourd