GASEOUS EXCHANGE & ITS CONTROL

Power point@lecture Slides Are Prepared By Biology Lecturer, KMPk

TOPICS 7.1 Gaseous exchange and control in mammals

PREVIOUS LESSON

CO2 transportation in blood

CO2 is transported between respiring tissues and the lungs in 3 different ways:
1 2 3

dissolved in blood plasma

as Carbamino haemoglobin

as bicarbonate ions (HCO3-)

OBJECTIVES
At the end of this topic, student should be able to: c. describe the oxygen dissociation curve of haemoglobin d. compare oxygen dissociation curve of haemoglobin and myoglobin e. explain Bohr effect due to partial pressure of carbon dioxide

Oxygen dissociation curves of haemoglobin

The curve shows the relative amounts of oxygen bound to haemoglobin exposed to solutions with different PO2

Oxygen dissociation curves of haemoglobin

When the partial pressure of oxygen is high as in lung capillaries, haemoglobin has a high affinity for oxygen to form oxyhaemoglobin
Campbell 9th edition, page 907

Oxygen dissociation curves of haemoglobin

When the partial pressure of oxygen is low as in respiring tissues, the oxyhaemoglobin dissociates and oxygen is liberated
Campbell 9th edition, page 907

Myoglobin
Compose of a single polypeptide chain with an iron atom that can bind to an O2 molecule Have higher affinity for oxygen than hemoglobin

Myoglobin

Function : store O2 in the muscle When O2 levels fall in muscle cells, myoglobin will contain O2 after the hemoglobin supplies have been exhausted
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Oxygen dissociation curves of haemoglobin & myoglobin in comparison

its O2 dissociation
curve is displaced well to the left of hemoglobin it only begins to release O2 when the partial pressure of O2 is below 20 mm Hg
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Oxygen dissociation curves of haemoglobin & myoglobin in comparison

in this way, it acts as a store of O2 in resting muscle (only releasing it when supplies of HbO2 have been exhausted) the myoglobin-oxygen dissociation curve is hyperbolic rather than sigmoid
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Oxygen dissociation curves of fetus & mother in comparison

At low PO2 levels, maternal hemoglobin gives up oxygen to fetal hemoglobin across the placenta The curve is shift to the left shows that fetal hemoglobin has a higher affinity for oxygen than mother at the same PO2.

Oxygen dissociation curves of fetus & mother in comparison

E.g: At 40mmHg, fetal hemoglobin is almost 90% saturated while maternal hemoglobin is only 75% saturated.

Bohr Effect/shift
- The effect of pH on
hemoglobin's affinity for oxygen - This is the result of H+ binding to hemoglobin

Bohr Effect/shift
It is shown graphically by a shift of the oxyhemoglobin dissociation curve to the right.

Bohr effect due to partial pressure of carbon dioxide

Partial pressure of O2 high in lung capillaries, haemoglobin has a high affinity for O2 to form oxyhaemoglobin Partial pressure of O2 low in respiring tissues, oxyhaemoglobin dissociates and O2 liberated

Bohr effect due to partial pressure of carbon dioxide

Partial pressure of CO2 increases, pH also decreases (increase of H+), haemoglobin has a low affinity for O2

Increase in CO2 pressure will shift the O2 dissociation curve to the right This effect known as Bohr Shift
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BOHR EFFECT
The red line on the graph represents the oxygen dissociation curve at a normal pH (pH = 7.4).

BOHR EFFECT
The green line represents the curve in the blood of exercising tissues, shifted to the right of the normal curve.

BOHR EFFECT
The black line represents the curve in the blood at the lungs, shifted to the left of the normal curve.

CONCLUSION
Remember!!! Higher PCO2 = Higher [H+] = Lower pH = Shift oxygen dissociation curve to the RIGHT

Questions
What is the Oxygen Dissociation Curves? What does a right shift indicate? What are the causes of a right shift? Why is the fetus haemoglobin curve shifted to the left? What is myoglobin?

NEXT LECTURE
17.2 Role of chemoreceptors in controlling breathing 17.3 Gaseous exchange and control in plants