Question 1
The graph shows the oxygen dissociation curves for haemoglobin of animals that live at high altitude and animals that live at low altitude.
What explains the oxygen dissociation curve at high altitude?
haemoglobin has a higher affinity for oxygen
haemoglobin releases oxygen more readily
the change in partial pressure of carbon dioxide causes a Bohr effect
the decrease in percentage of carbon dioxide causes the curve to shift to the left
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Question 2
Haemoglobin can bind to carbon dioxide, carbon monoxide, and oxygen.
Which statement about the binding sites of haemoglobin is correct?
carbon dioxide and carbon monoxide bind to one site, oxygen binds to a different site
carbon dioxide and oxygen bind to one site, carbon monoxide binds to a different site
carbon monoxide and oxygen bind to one site, carbon dioxide binds to a different site
carbon monoxide, oxygen and carbon dioxide all bind to different sites
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Question 3
An increase in carbon dioxide in human blood shifts the oxyhaemoglobin dissociation curve to the right.
What is the explanation for this effect?
an increase in carbon dioxide concentration increases the ventilation rate
carbon dioxide is more soluble than oxygen and displaces it
diffusion of carbon dioxide between the alveoli and the blood is more rapid
increasing the H+ concentration decreases haemoglobin affinity for oxygen
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Question 4
Which statement describes the Bohr effect?
in high partial pressure of oxygen and high partial pressure of carbon dioxide, the affinity of haemoglobin for oxygen increases
in high partial pressure of oxygen and low partial pressure of carbon dioxide, the affinity of haemoglobin for oxygen decreases
in low partial pressure of oxygen and high partial pressure of carbon dioxide, the affinity of haemoglobin for oxygen decreases
in low partial pressure of oxygen and low partial pressure of carbon dioxide, the affinity of haemoglobin for oxygen is unchanged
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Question 5
What is the reason for an increase in red blood cells in humans at high altitudes?
to compensate for the low percentage saturation of haemoglobin
to enable haemoglobin to unload more oxygen in the tissues by the Bohr effect
to ensure that haemoglobin is almost 90% saturated when it reaches the tissues
to increase the number of mitochondria in the blood for ATP production
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Question 6
What is the primary structure of haemoglobin made up of?
alpha helices
beta sheets
polypeptide chains
haem groups
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Question 7
Which statement best describes cooperative binding in haemoglobin?
the binding of the first oxygen molecule has no effect on the binding of subsequent oxygen molecules
the binding of the first oxygen molecule makes it harder for subsequent oxygen molecules to bind
the binding of the first oxygen molecule makes it easier for subsequent oxygen molecules to bind
the binding of oxygen molecules is completely independent of other molecules
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Question 8
Why does haemoglobin offload more oxygen into tissues with high metabolism?
because these tissues have a lower pH
because these tissues have a higher pH
because these tissues have a lower temperature
because these tissues have a higher temperature
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Question 9
What effect does a low pH have on the affinity of haemoglobin for oxygen?
it increases the affinity
it decreases the affinity
it does not affect the affinity
it reverses the affinity
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Question 10
Haemoglobins with a high affinity for oxygen are characterised by their ability to do what?
take up oxygen more easily and release it more easily
take up oxygen more easily but release it less easily
take up oxygen less easily and release it more easily
take up oxygen less easily but release it less easily
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