/GASEOUS EXCHANGE

( QUESTION 1 )

The diagram below shows reaction occurring in the red blood cells of mammals when it arrives at the tissue.

(a) Name the substances labelled R, S, T and U [ 4m ]

R : ……………………………………………………………………………………

S : ……………………………………………………………………………………

T ; ……………………………………………………………………………………

U : ……………………………………………………………………………………
(b) Explain the steps that occur at stage I, II, III and IV in the diagram [ 6m ]

I : ………………………………………………………………………………………………………………..

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II : ………………………………………………………………………………………………………………

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III : ………………………………………………………………………………………………………………

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IV : ……………………………………………………………………………………………………………….

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 /GASEOUS EXCHANGE
Question 1

(a) R – Hydrogecarbonate ion S – carbonic anhydrase

T - Clˉ U – haemoglobin acid

(b) I – carbon dioxide diffuse into the red blood cell from the tissue that has a higher partial pressure gradient.

II - carbonic acid ionize easily to form H+ and HCO3ˉ with the help of carbonic anhydrase.

III- H+ ions formed CO2 combine with oxyhaemoglobin liberating the O2. The haemoglobin becomes
haemoglobin acid.

IV – HCO3ˉ ions easily diffuse out from the red blood cells as the membrane is very permeable to them.Clˉ
diffuse into the red blood cells to balance the increase in positive charges outside.
 /GASEOUS EXCHANGE
QUESTION 2

The diagram below shows the oxygen dissociation curves of myoglobin, mother haemoglobin and foetal
haemoglobin.

(a) Name the curves labelled X, Y and Z. [ 3m ]

X : …………………………………………………………………………………………….

Y : …………………………………………………………………………………………….

Z : …………………………………………………………………………………………….
(b) Compare curves X and Y, what is the physiological significance of difference between X and Y? [[ 2m ]

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(c) Compare curves Y and Z, what is the physiological significance of difference between Y and Z? [ 2m ]

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(d) What is the effect of carbon dioxide on the oxygen dissociation curve for the mother?
Explain the effect and its significance. [ 3m ]

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 GASEOUS EXCHANGE

Question 2

(a) X – The oxygen dissociation curve of myoglobin

Y - The oxygen dissociation curve of foetal
Z - The oxygen dissociation curve of mother or adult

(b) – The disscociation curve of X is to the left of thet of foetal haemoglobin indicating that it has a higher affinity
for oxygen than that of foetus.

- This would enable oxygen to be stored in the developing muscle of the foetus and to be used when
partial pressure of oxygen runs low.

(c) – The dissociation curve of Y ( foetal haemoglobin ) is to the left of that of mother’s haemoglobin indicating
that it has a higher affinity for oxygen than that of the mother’s.

- This would enable the foetal haemoglobin to obtain oxygen from the mother’s haemoglobin at the
placenta where the partial pressure of oxygen is low.

(d) -carbon dioxide would shift the oxygen dissociation curve to the right causing the oxyhaemoglobinto
dissociate its oxygen even at high partial pressure of oxygen.

- The effect is caused by cabon dioxide when dissolved in the blood forming H+ ions that effect the oxy-
haemoglobin to release its oxygen.

- The significance is that oxy-haemoglobin would release its oxygen in areas with high carbon dioxide
concentration where the cells are most avtive and require the most oxygen .
 /GASEOUS EXCHANGE
QUESTION 3

The transport of carbon dioxide by blood is shown in the diagram below.

(d) State three ways how carbon dioxide is transported in blood.

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[ 3 marks ]
(b) What is meant by chloride shift?

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[ 2 marks ]
I(i) Name enzyme A.

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[ 1 marks ]
(ii) Write an equation involving carbon dioxide, X and Y.

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[ 2 marks ]
(d) State two role of haemoglobin in maintaining the pH of blood.

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[ 2 marks ]
 GASEOUS EXCHANGE

Question 3
(a) -As bicarbonate ions ( hydrogencarbonate ions)(HCO3-)
-As carbaminohaemoglobin
-As dissolved carbon dioxide in plasma.

(b) -When the negatively charged hydrogencarbonate ions diffuse out into the plasma, the
inside of the red blood cell will become positively charged.
-The positive charge is immediately restored (neutralized) by the entry of chloride ions
(Cl-) from the plasma.

(c) (i) Carbonic anhydrase

(ii) CO2 + H2O H2CO3

(d) -High concentration of CO2 causes blood pH to decrease., this reduces the affinity of
haemoglobin for O2.
-Hence,causes unloading of O2 in capillaries of tissues.
-X acts as a buffer by combining with H+ ions to form haemoglobinic acid.
This is important in preventing blood from becoming too acidic.
 /GASEOUS EXCHANGE
( QUESTION 4 )

Figure 3.1 shows the oxygen dissociation curve for adult haemoglobin under the normal condition.

(a) Explain briefly why the dissociation curve has a sigmoid or S – shaped. [3m]

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(b) Sketch the oxygen dissociation curve
(i) P : for adult haemoglobin under high partial pressure of carbon dioxide
(ii) Q : for fetus haemoglobin under normal condition on the figure 3.1 [2m]

(c) Explain any physiological advantage resulting from the altered dissociation curve in the presence of a high
level of carbon dioxide. [3m]

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(d) Suggest why an expectant mother is advised to give up smoking. [2m]

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 GASEOUS EXCHANGE
ANSWER : QUESTION 4

(a) Initially oxygenation of haemoglobin is low

But after combining with one molecule of oxygen, hb changes it shapes
Exposing the other haem group to oxygen
Thus, making subsequent oxygenation of hb easier

(b) Q : curve located at the left

P : curve located at the right

(c) A high level of carbon dioxide indicate an area where cells are actively respiring
The curve is shifted to right // Bohr effect
The affinity of hb for oxygen decreases
The unloading tension of curve is highest
Enabling oxygen to be easily released to the acyive cells.

(d) Carbon dioxide in the smoke combines with hb reduces its oxygen carrying capacity insufficient oxygen is
supplied to the fetus.
 GASEOUS EXCHANGE
( QUESTION 5 )

The table below shows the percentage of saturation haemoglobin (Hb) resulting from a range of partial pressure of
oxygen (PO2) at two different concentration of carbon dioxide (mmHg)

PO2 / mmHg % saturation of Hb at % saturation of Hb at

PCO2 = 40 mmHg PCO2 = 80 mmHg
10 11 8
20 38 22
30 59 42
40 75 60
50 83 71
60 90 81
70 94 88
80 98 95
90 99 98
100 99 99

(a) Plot a graph on a single pair of axes to show these different concentration of carbon dioxide [2m]

(b) From the graph, what is the percentage saturation of Hb when PO2 is 55 mmHg?

(i) At PCO2 40 mmHg : ………………………………………………………….. [1m]

(ii) At PCO2 80 mmHg : …………………………………………………………. [1m]

(c) What is your inference from the above answer? [1m]

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(d) State two main features of the respiratory pigment, haemoglobin. [2m]

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(e) Briefly explain the structure of erythrocyte in relation to its function. [3m]

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 /GASEOUS EXCHANGE
QUESTION 6

The diagram below illustrates gaseous exchange in respiring tissues.

(a) Fill in the blank boxes in the diagram with appropriate labels, symbols or formulae.
(b) Suggest the process involved in the movement of substances in 1, 4, 5 and 7.

1 : …………………………………………………………………………………………………….

4 : …………………………………………………………………………………………………….

5 : ……………………………………………………………………………………………………

7 : ……………………………………………………………………………………………………..
(c) Name the enzyme that is involved in process 2.

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(d) Name process 3

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(e) Name the phenomenon shown in process 5 and state its significance

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(f) Why is oxygen transferred in process 6 ?

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ANSWER : QUESTION 6

(a)

.(b) Diffusion

.(c) Carbonic anhydrase

.(d) Dissociation / Ionises

.(e) Chloride shift

To maintain the electrochemical neutrality

.(f) By releasing oxygen,

Haemoglobin acts as a buffer, accepting H+ ions to form haemoglobinic acid
(reduced haemoglobin, HHb )
 GASEOUS EXCHANGE
QUESTION 7

The graph below shows the haemoglobin dissociation curves for two animals, i.e the elephant and the mouse.

(a) State three important properties for any respiratory pigment such as haemoglobin.

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(b)(i) Explain the effect of reducing partial pressure of oxygen on the percentage saturation of haemoglobin in
the elephant.
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(iii) Describe the differences between the dissociation curves for the elephant and the mouse.

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(iii). How would the differences be related to the sizes of the two animals?

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(c). The following graph shows the effect of acid on the oxygen dissociation curve for the mouse (the Bohr effect)

(i). Comment on the effect of the increase in acidity on the dissociation curve for the mouse.

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(ii). Explain why respiring tissues caused a change in pH.

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(iii). Explain the physiological advantage of the Bohr effect.

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 QUESTION 7
ANSWER

(a) 1. Has a high affinity for oxygen at a high oxygen tension such as would be found in the lung.
2. Has a low affinity for oxygen at a low oxygen tension such as would be found in tissues
3. Combination of respiratory pigments with oxygen is reversible.

(b) (i) – At an oxygen partial pressure of 10 kPa, haemoglobin is 100% saturated with oxygen.
- A slight decrease in the partial pressure of oxygen brings about slight fall in the percentage of
saturation of haemoglobin with oxygen.
- Over the steep part of the curve, a small decrease in the partial pressure of oxygen brings
about a large fall in the percentage of saturation of haemoglobin with oxygen.

(ii) - The dissociation curve for the elephant is displaced to the left
- The haemoglobin of elephant picks up oxygen more readily but releases it less readily
- The dissocoiation curves for the mouse is displaced to the right.
- The haemoglobin of the mouse picks up oxygen less readily but releases it more easily

(iii) -The size of elephant is large, it has a small surface area to volume ration.
- The rate of heat loss to the surrounding is low and therefore has a low metabolic rate.
- Unloading of oxygen to the tissues can occur slowly.
- The mouse has a large surface area to volume ratio.
- The rate of heat loss to the surrounding is high metabolic rate.
- Haemoglobin unloads oxygen readily to the tissues.

(c) (i) - An increase in the acidity shifts the dissociation curve to the right.
(ii). – Respiring tissues release carbon dioxide which will combine with water to form carbonic acid
- The carbonic acid then dissociate into hydrogen and hydrogen carbonate ions.
- Hydrogen ions lower the pH value.

(iii). – By having the dissociation curve shifted to the right, the haemoglobin’s affinity for oxygen is reduced.
- More oxygen is released to the respiring tissues and more energy is produced.
- An increase in metabolic activity increases body temperature.
- This displace the dissociation curve further to the right, releasing more oxygen to respiring
tissues.
 /GASEOUS EXCHANGE
QUESTION 7

Below are three dissociation curve of haemoglobin of three different mammal. Compare and discuss the differences
between:

Fig (i) Oxygen dissociation curve for the haemoglobin of three mammals.

(i) The dissociation curve of Llama and human haemoglobin

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(ii) The dissociation curve of mouse and human haemoglobin.

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ANSWER : QUESTION 8

(a) (i) - Llama is an animal living at high altitude where there is a reduced air pressure.
- At this altitude The PO2 is lower compared to the sea level.
- The difference of PO2 in the air and the llama’s lungs is lowered thus less oxygen can diffuse
across the alveoli.
- Thus this makes it difficult to load haemoglobin.
- The llama’s haemoglobin therefore has a high affinity of oxygen to compensate for this.
- Therefore the dissociation curve for llma is to the left of the human haemoglobin.

(ii)- Mouse is a small animal, so it has a larger surface area to volume ratio than human.
- The mouse loses heat rapidly.
- To compensate for this it has a higher metabolic rate than human to help generate heat.
- To keep tissues supplied with oxygen the haemoglobin of the mouse has a lower affinity for
oxygen and therefore unloads the gas quickly to the tissues.
- The reduced affinity does not adversely affect the loading of haemoglobin as the partial
pressure of oxygen of air is more than enough to fully saturate the haeoglobin.
 /GASEOUS EXCHANGE
QUESTION 9

The graph below shows a dissociation curve of haemoglobin and myoglobin and in human. Haemoglobin and
myoglobin in human. Haemoglobin and myolobin are two respiratory pigments, which differ in site , structure and
function in our body.

(a) Discuss the differences in site, structures and the functions of haemoglobin and myoglobin.

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(b) Explain the different shape of dissociation curve of haemoglobin and myoglobin.

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(c) Explain the dissociation curve of myoglobin above the partial pressure of oxygen of 20 mmHg.

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QUESTION 9 – ANSWER

(a). - Haemoglobin is found in red blood cells but myoglobin is found in muscles.

- Haemoglobin consist of four subunits of polypeptide, 2-α and 2β polypeptide however moglobin is made up
of only one polypeptide chain.

- In each subunit of haemoglobin there is a haem group that can binds with one oxygen molecules.

- Thus one haemoglobin can carry a maximum of 4 oxygen molecules.

- Since myoglobin contain only one haem group thus it can binds only with one molecule of oxygen.

- Haemoglobin carry oxygen in the bloodstream but myoglobin keeps oxygen in muscles.

(b). The myoglobin ‘s oxygen dissociation curve is hyperbolic in shape but the haemoglobin curve is sigmoid

- At low PO2 below 20mmHg, the percentage saturation of myoglobin with oxygen decreases sharply from
75% to 0%.

- However above 20 mmHg the % saturation of myglobin with oxygen remains high and almost constant at
the range of 75% to 85%.

- Sigmoid curve for haemoglobin is due to its cooperative binding effect whereby when one molecule of o
oxygen has bounded to the haem, the other three are able to bind at a faster rate.

- This happens especially at low partial pressure of oxygen.

(c). - The blood that flows through resting or moderately active muscle has the partial pressure of oxygen above
20 mmHg.

- As the oxygen demand is not critical, the myoglobin retain as much as 75% to 85% of its oxygen.

- Its affinity for oxygen is very high.

 /GASEOUS EXCHANGE IN HUMAN
QUESTION 9
Figure 3.1 shows the oxygen dissociation curve for adult haemoglobin at different partial pressures of carbon dioxide
( pCO2 / kPa)

(a)(i) Explain how the properties of the haemoglobin molecule cause the oxygen dissociation curves shown in
Figure 3.1 to be sigmoid ( S- shaped ) [3m]

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(ii)Using the information shown in Figure 3.1, describe the effect of the increase in the partial pressure of carbon
dioxide on the percentage saturation of haemoglobin. [2m]

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(iii)Explain how the increase in the partial pressure of carbon dioxide will cause the effect shown in Figure 3.1. [2m]

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(iv)During exercise, the partial pressure of carbon dioxide increases, Explain the important of the effect of this
increase. [2m]

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Gaseous exchange in human
Question 9

(a) (i) Oxygen binds to the haem groups ; R iron

First oxygen molecule, binds slowly / harder to bind /
Distorts shape of molecule / allosteric
Easier for the next oxygen to bind / next oxygen molecule, binds faster
Curve therefore steep in middle

(ii). -As the partial pressure of carbon dioxide increases, the saturation of Hb with oxygen decreases /
desaturation increases
-Curve shift to the right

(iii). -increased CO2 levels release hydrogen / hydrogen carbonate form

-decreases pH in the plasma
-causes the release of the oxygen by the Hb / lowers affinity for oxygen

(iv). -during exercise rate of respiration increases as demand for oxygen increases
-more oxygen released from Hb.
 /GASEOUS EXCHANGE IN HUMAN
QUESTION 11

The figure below shows the relationship between tissue cells and capillaries in the transport of carbon dioxide.

(a) Name the process and the causes of each process labeled A, C and D [6m]

A :………………………………………………………………………………………………………………………...

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C : ……………………………………………………………………………………………………………………………

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D : ………………………………………………………………………………………………………………………………

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(b) Explain what happens in the red blood cell. [2m]

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(c) At point B, why does HCO3 move out of the red blood cell? [2m]

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GASEOUS EXCHANGE IN HUMAN
QUESTION 11

(a) A : Diffusion
CO2 level in the active cells is more concentrated. So, it diffuses into red blood cells

C : Dissolve
CO2 reacts with water in the red blood cells to form carbonic acid

D : Dissociation
Carbonic acid immediately dissociate to form a hydrogen carbonate ion and a proton

(b) Carbon dioxide react with water to form carbonic acid

The reaction in water is very slow. But blood cell contain carbonic anhydrase which catalyses the reaction
with water

(c) Hydrogen carbonate is very soluble in water

If there is too much hydrogen carbonate in the red blood cells, it will diffuse out into the blood plasma
through an ion channel
This channel carries one chloride ion into the cell for every hydrogen carbonate ion it carries out, and this
helps to keep the charge in the cell cinstant.