Transport of oxygen by haemoglobin Flashcards

1
Q

What does the oxygen dissociation curve show?

A

The oxyhaemoglobin dissociation curve shows the relationship. between the saturation of haemoglobin with oxygen and the partial pressure of oxygen

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2
Q

Why does haemoglobin not bind oxygen evenly at different partial pressures?

A

Haemoglobin’s affinity for oxygen changes depending on the partial pressure, leading to the characteristic S - shape of the oxygen dissociation curve

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3
Q

What is the shape of the oxygen dissociation curve?

A

A sigmoid (S-shaped) curve

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4
Q

Why is the oxygen dissociation curve initially shallow at low partial pressures of oxygen?

A

The first oxygen molecule binds slowly because haemoglobin’s shape makes it difficult for oxygen to associate

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5
Q

Why is it difficult for the first oxygen molecule to bind to haemoglobin?

A

The polypeptide subunits are closely united, making it hard for the first oxygen molecule to bind

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6
Q

What happens at low oxygen concentrations, and how is this shown on the oxygen dissociation curve?

A

Little oxygen binds to haemoglobin, so the initial gradient of the oxygen dissociation curve is shallow

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7
Q

How does the bind of the first oxygen molecule affect the haemoglobin molecule?

A

It changes the quaternary structure, making it easier for the other subunits to bind oxygen

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8
Q

What is positive cooperativity in haemoglobin, and how does it affect the oxygen dissociation curve?

A

Positive cooperativity is when the binding of one oxygen molecule makes it easier for the next to bind, so a smaller increase in partial pressure is needed for the second oxygen molecule to bind

On the oxygen dissociation curve, the gradient of the curve steepens as oxygen binds more easily

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9
Q

Why does the binding of the fourth oxygen molecule become harder?

A

Most binding sites are already occupied, making it less likely that an oxygen molecule will find an empty site

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10
Q

Why does the curve level off at high partial pressures of oxygen?

A

Most haemoglobin molecules are already saturated , so additional oxygen molecules find fewer available binding sites

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11
Q

How does the difficulty of binding the fourth oxygen molecule affect the oxygen dissociation curve?

A

The gradient decreases, and the graph flattens off

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12
Q

How does the shape of haemoglobin change?

A

The shape of any one type of haemoglobin can change under different conditions, affecting its oxygen affinity

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13
Q

What does the existence of different types of haemoglobin result in?

A

A large number of different oxygen dissociation curves, each with a similar shape but differing positions on the axes

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14
Q

How does the position of the oxygen dissociation curve relate to haemoglobin’s affinity for oxygen?

  1. Left shifted curve?
  2. RIght shifted curve?
A

A left shifted curve results in haemoglobin having a higher affinity for oxygen, meaning it loads oxygen easily but unloads it less easily

A right shifted curve results in haemoglobin having a lower affinity for oxygen, meaning it can load oxygen less easily but unload it more easily

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15
Q

How does carbon dioxide affect haemoglobin’s affinity for oxygen?

A

Haemoglobin has a reduced affinity for oxygen in the presence of carbon dioxide, meaning it releases oxygen more readily

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15
Q

How does the Bohr effect explain haemoglobin’s behaviour at the gas exchange surface (lungs)?

A

At the lungs, where carbon dioxide concentration, hemoglobin’s affinity for oxygen increases, allowing oxygen to load rapidly. The oxygen dissociation curve shifts to the left

15
Q

What is the Bohr effect?

A

The Bohr effect describes how the greater the concentration of carbon dioxide, the more readily haemoglobin releases its oxygen

16
Q

How does the Bohr effect explain haemoglobin’s behaviour in rapidly respiring tissues (muscles)

A

In muscles, where carbon dioxide concentration is high, haemoglobin’s affinity for oxygen decreases, allowing oxygen to unload readily into the muscle cells. The oxygen dissociation curve shifts to the right

17
Q

Why does increased carbon dioxide concentration reduce haemoglobin’s affinity for oxygen?

A

Dissolved carbon dioxide is acidic, and the lower pH causes haemoglobin to change shape, making it more likely to release oxygen