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Oxygen dissociation curves

  • 2 things to know
  • Papers 1, 2 and 3

Overview

Recall questions on reading the sigmoid curve, comparing foetal and adult haemoglobin, and myoglobin.

What you need to know

Answer each one before you reveal it.

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Key term

What polypeptide chains make up fetal haemoglobin, and how does this differ from adult haemoglobin?

Key term

What is the partial pressure of oxygen like in fetal blood at the placenta?

Questions from this subtopic

Each one with the model answer underneath.

  1. 1

    What is the shape of the oxygen dissociation curve for haemoglobin, and what does this shape reflect?

    Model answer

    Sigmoidal (S-shaped); it reflects cooperative binding of oxygen.

  2. 2

    What happens to haemoglobin saturation at intermediate partial pressures of oxygen?

    Model answer

    There is a rapid increase in saturation (the steep part of the curve).

  3. 3

    Why does the oxygen dissociation curve plateau at high partial pressures of oxygen?

    Model answer

    Because haemoglobin approaches saturation (close to 100%) and cannot bind significantly more oxygen.

  4. 4

    What is the physiological significance of the plateau region of the oxygen dissociation curve at high partial pressures?

    Model answer

    It ensures haemoglobin remains nearly fully saturated even if alveolar oxygen levels fall slightly.

  5. 5

    Why is the steep portion of the oxygen dissociation curve at lower partial pressures physiologically important?

    Model answer

    It allows efficient unloading of oxygen in respiring tissues where oxygen demand is high.

  6. 6

    What is the shape of myoglobin's oxygen dissociation curve, and why does it differ from haemoglobin's?

    Model answer

    Hyperbolic; because myoglobin does not exhibit cooperative binding.

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ALag phase shows no increase.
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