Movement of Carbon Dioxide & Oxygen Flashcards

1
Q

What happens to CO2 after the respiration of tissue?

A

The CO2 dissolves into tissue fluid, and then into the blood plasma.

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2
Q

What does CO2 do once dissolved in the blood plasma?

A
  • 5% remains in plasma as dissolved CO2
  • 95% diffuses into the cytoplasm
  • 10-20% of the CO2 in the cytoplasm binds with amino groups in the Hb, forming carbaminohaemoblin
  • The remaining 75-85% forms hydrogen carbonate ions in the erythrocyte’s cytoplasm
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3
Q

How do hydrogen carbonate ions form in the erythrocyte’s cytoplasm?

A
  • CO2 combines with water to form carbonic acid (CO2 + H2O –> H2C03)
  • Carbonic acid dissociates, releasing hydrogen ions and hydrogen carbonate ions (H2CO3 –> H+ + HCO3-)
  • HCO3- diffuses out of the erythrocyte and into the blood plasma
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4
Q

What enzyme catalyses the formation of carbonic acid?

A

Carbonic anhydrase

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5
Q

What happens when the hydrogen carbonate ions diffuse out of the erythrocytes?

A

The chloride shift - chloride ions diffuse into the erythrocytes to maintain charge / electrochemical balance

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6
Q

What happens to the H+ ions released by the dissociation of carbonic acid?

A

They are taken up by Hb to prevent the erythrocyte from becoming acidic. The Hb acts as a buffer to maintain ph.

This forms haemoglobinic acid.

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7
Q

What are the adaptations of erythrocytes?

A
  • biconcave disc - large SA for exchange
  • no nucleus or organelles associated with protein synthesis (ribosomes, rough ER, golgi)
  • no mitochondria in mature cells
  • contains haemoglobin
  • approx 7 micrometers diameter - roughly same as capillaries - shorter exchange pathway
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8
Q

What happens to oxygen when it binds with haemoglobin?

A

It is taken out of solution, meaning a steep concentration gradient is maintained.

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9
Q

What is haemoglobin?

A

A large globular, conjugated protein - made up of 4 peptide chains, each containing a haem prosthetic group.

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10
Q

What is positive cooperativity / cooperative binding?

A

When one oxygen molecule binds to a haem group, the haemoglobin molecule changes shape to make it easier for the next oxygen molecules to bind.

The same happens when removing oxygen molecules.

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11
Q

What is meant by partial pressure?

A

The concentration of a specific chemical when in a mixture of gases.

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12
Q

What is an oxygen dissociation curve?

A

A curve showing the percentage saturation of haemoglobin in the blood against the partial pressure for oxygen.

It shows the affinity of haemoglobin for oxygen.

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13
Q

What is meant by affinity for oxygen?

A

The strength of the interaction between haemoglobin and oxygen.

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14
Q

What is the case on an oxygen dissociation curve at low partial pressure of oxygen?

A

At low pO2, few haem groups are bound to oxygen, so haemoglobin does not carry much oxygen.

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15
Q

What is the case on an oxygen dissociation curve at higher partial pressures of oxygen?

A

At higher pO2, more haem groups are bound to oxygen, making it easier for more oxygen to be picked up - the percentage saturation of haemoglobin increases.

Haemoglobin becomes very saturated at high pO2, as all haem groups have bound with oxygen.

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16
Q

What is the Bohr effect?

A

As the partial pressure of CO2 rises, haemoglobin gives up oxygen more easily - this means the oxygen dissociation curve moves to the right.

17
Q

Why is the Bohr effect important?

A
  • in active tissues with a high pCO2, haemoglobin gives up oxygen more readily
  • in the lungs, where proportion of CO2 in the air is relatively low, oxygen binds to haemoglobin more easily
18
Q

Why is fetal haemoglobin different to adult haemoglobin?

A

Fetal haemoglobin has a higher affinity for oxygen than adult haemoglobin.
- oxygenated maternal blood runs close to deoyxgenated fetal blood.

If fetal haemoglobin’s affinity for oxygen was lower, then little to no oxygen would be transported into the fetal blood.