Lesson 3.3.4.1.2

3.3.4.1.2 Haemoglobin and oxygen transport Quiz: AQA Biology, Unit 3

20 questions

Written by Revision Ninja · Last reviewed 11 October 2026

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Lesson 3.3.4.1.2, Haemoglobin and oxygen transport: 20 multiple choice questions for the AQA Biology (7402), Unit 3: Organisms exchange substances with their environment, written with Revision Ninja.

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The 20 questions

  1. How many polypeptide chains make up a single haemoglobin molecule?

    • Four
    • Two
    • Six
    • Three

  2. What effect does high carbon dioxide concentration have on haemoglobin's oxygen affinity?

    • Decreases affinity
    • Prevents binding
    • No effect
    • Increases affinity

  3. What property of haemoglobin causes its oxygen dissociation curve to be sigmoid?

    • Cooperative binding
    • Irreversible binding
    • Competitive inhibition
    • Allosteric degradation

  4. What condition in the lungs promotes oxygen loading onto haemoglobin?

    • High carbon dioxide
    • Low pH level
    • Low oxygen pressure
    • High oxygen pressure

  5. What condition in respiring tissues promotes oxygen unloading from haemoglobin?

    • Low carbon dioxide
    • Low oxygen pressure
    • High pH level
    • High oxygen pressure

  6. How is the haemoglobin of animals living in low-oxygen environments adapted?

    • Higher oxygen affinity
    • Fewer polypeptide chains
    • Lower oxygen affinity
    • No haem groups

  7. What does 60% oxygen saturation of haemoglobin represent?

    • 60% remaining capacity
    • 60% bound sites
    • 60% haemoglobin destroyed
    • 60% dissolved oxygen

  8. How does the Bohr effect benefit actively respiring muscle tissue?

    • Prevents oxygen unloading
    • Increases oxygen loading
    • Decreases oxygen unloading
    • Increases oxygen unloading

  9. What does a leftward shift in an oxygen dissociation curve indicate?

    • Lower oxygen affinity
    • Lower pH level
    • Higher carbon dioxide
    • Higher oxygen affinity

  10. Which protein in red blood cells binds to oxygen for transport?

    • Haemoglobin
    • Carbonic anhydrase
    • Fibrinogen
    • Myoglobin

  11. How does the oxygen affinity of fetal haemoglobin compare to adult haemoglobin?

    • Higher
    • Lower
    • Zero
    • Identical

  12. What shape is the oxygen dissociation curve for human haemoglobin?

    • Inverted U
    • Linear
    • Sigmoid
    • Hyperbolic

  13. Which pigment is found in muscle tissue and has a higher affinity for oxygen than haemoglobin?

    • Myoglobin
    • Chlorophyll
    • Melanin
    • Carotene

  14. What is the main effect of a low blood haemoglobin concentration?

    • Reduced oxygen capacity
    • Higher blood pH
    • Increased oxygen capacity
    • Increased blood pressure

  15. Where in the human body does haemoglobin load oxygen?

    • Kidneys
    • Respiring muscles
    • Liver
    • Lungs

  16. What effect does an increased temperature have on the oxygen dissociation curve?

    • Vertical shift
    • No shift
    • Rightward shift
    • Leftward shift

  17. What happens to haemoglobin at the lower oxygen partial pressure found in respiring tissues?

    • It binds oxygen
    • It denatures
    • It releases oxygen
    • It breaks down

  18. Which change causes a shift of the oxyhaemoglobin dissociation curve to the right?

    • Increased blood pH
    • Decreased temperature
    • Decreased carbon dioxide
    • Increased carbon dioxide

  19. Why do different animal species possess haemoglobins with different oxygen-binding affinities?

    • Random genetic mutation
    • Adaptation to environment
    • Differences in temperature
    • Varying blood pressure

  20. Why is myoglobin effective at storing oxygen in muscle tissue at low partial pressures?

    • Higher oxygen affinity
    • Lower oxygen affinity
    • Four binding sites
    • Quaternary structure

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