haemoglobin and oxygen transport

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26 Terms

1
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what are two adaptations of a red blood cell and how do they allow large amounts of oxygen in a short time?

  • (biconcave shape causes RBCs to) have a large S.A to volume ratio for diffusion

  • they are flat/thin so oxygen can reach all of the haemoglobin / centre rapidly

2
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what are haemoglobins?

a group of globular proteins with a quaternary structure

3
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what do haemoglobins consist of?

  • four polypeptide chains linked to form a spherical molecule

  • each polypeptide chain is associated with a haem group containing a Fe2+ ion

  • Fe2+ can be combined with one O2 molecule

4
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what is the role of harmoglobin?

oxygen transport

5
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where does oxygen bind to haemoglobin in the body and what is formed when they bind?

  • in the lungs

  • forms oxyhaemoglobin

6
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what is the process called when oxygen binds to haemoglobin?

association/loading

7
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what is the process called when oxygen leaves haemoglobin?

dissociation/unloading

8
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what does the term affinity of haemoglobin for oxygen mean?

the ability of haemoglobin to attract, or bind to oxygen

9
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what factors affect haemoglobin's affinity for oxygen?

  • the partial pressure of oxygen (pO2)

  • haemoglobin saturation

  • the partial pressure of carbon dioxide (pCO2)

10
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what is partial pressure?

a measure of concentration of a specific gas within a mixture of gases

11
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where does haemoglobin have a high affinity and a low affinity for oxygen?

  • high - oxygen rich areas, e.g. lungs

  • low - oxygen deprived areas, e.g. respiring tissues

12
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what is cooperative binding?

the binding of each oxygen changes the shape of the haemoglobin, making it easier for the next to bind

13
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how does pO2 affect haemoglobin saturation?

higher pO2 increases haemoglobin saturation

14
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what is the Bohr effect?

reduced pH decreases haemoglobin's affinity for oxygen

15
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how does increasing partial pressure of carbon dioxide (pCO2) affect haemoglobin's affinity for oxygen?

decreases affinity, promoting oxygen dissociation

16
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what effect does high partial pressure of carbon dioxide (pCO2) have on the oxygen dissociation curve?

it shifts to the right

17
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in which direction does the oxygen dissociation curve shift during high respiration and what is the advantage of this?

it shifts right

  • haemoglobin has a lower affinity for oxygen

  • so more oxygen is available for respiration

18
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how does aerobic respiration lead to a change in plasma pH? (3)

  • during aerobic respiration carbon dioxide is produced

  • CO2 dissolves in the blood plasma to form carbonic acid

  • this causes an increase in H+ ion concentration

19
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what is the advantage to tissue cells of a reduction in haemoglobin’s affinity for oxygen when plasma pH deceases?

  • low pH is due to the high rate of respiration

  • cells need more oxygen

  • so more oxygen is released

20
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how is oxygen in a RBC made available for respiration in active tissues?

  • low pH is due to increased CO2 during respiration

  • this increases dissociation of haemoglobin

  • oxygen diffuses from RBC to tissues

21
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what is the haemoglobin affinity of a foetus in the womb like?

  • higher affinity

  • dissociation curve is shifted to the left

22
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explain the advantage of the curve of foetal haemoglobin being different to an adult (3)

  • foetal haemoglobin have a higher affinity for oxygen

  • so becomes saturated at a lower partial pressure

  • at partial pressures when adult haemoglobin dissociates, foetal haemoglobin takes up oxygen

23
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what is the haemoglobin affinity of animals living in low oxygen environments like?

  • higher affinity

  • dissociation curve is shifted to the left

24
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explain the advantage of the curve of animals living in low oxygen environments being different to animals living in high altitudes (3)

  • high altitudes have a low partial pressure of oxygen

  • so have a high affinity of haemoglobin with oxygen

  • so sufficiency oxygen is supplied to cells/tissue

25
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what is the haemoglobin affinity of small organisms with high SA:V/high metabolic rate like?

  • lower affinity

  • dissociation curve is shifted to the right

26
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why do high metabolic rate animals have haemoglobin with low oxygen affinity?

allows easier oxygen unloading for high demand