CHAPTER

GASEOUS
EXCHANGE AND
IT5 CONTROL

SUBJECTIVE OUESTIONS

7.',1 Gaseous Exchange and Control in Mammals

Explain the structure of haemoglobin.

ffi$
I ttllt
Haemoglobin is a conjugated protein.

a Haemoglobin is a reddish-purple pigment found inside red blood cel1s.

a Haemoglobin is a quartenary protein that is made up of fbur polypeptide chains,
2a-chains and 2B-chains.
o The polypeptide chains make up the globin part of the molecule.
a Each of these polypeptide chains is associated with a haem group with an iron(Il)
ion at its centre.
a Each iron ion can bind with one oxygen molecule (2 oxygen atoms).
a So, one haemoglobin molecule can bond with fbur oxygen molecules.
a Haemoglobin has a high affinity for oxygen.
a Haemoglobin binds rapidly with oxygen when oxygen concentration is high, as in
the lungs. It releases oxygen when oxygen concentration is low, as in respiring
tissues.

Hb+40,-HbO,
' At tissues, oxygen is more concentrated in the blood than in the tissues and so
diffuses out of the capillaries into the tissues.
' In the same way carbon dioxide is more concentrated in the tissues, so it {iffuses
out of the tissues and moves into the blood.

What is an oxygen dissociation curve for haemoglobin? Plot the curve and state
the shape ofthe curve.

' It is a curve that shows the relationship between various partial pressures of oxygen
and the percentage of oxygen saturation of haemoglobin.
 86 Gaseous Exchange and lts Control

100
.g
3o
980
E
a)
-E oo
o
c
e40
6
-
320
o

20 40 60 80 100
po2 (mmHg)

. Sigmoid
f'G€iltRiEht
Students often draw a hyperbolic curve instead of a sigmoid.

Explain the importance of the S shape of an oxygen dissociation curve.

'1*s
f Hilr
. The binding of oxygen is slow atthe beginning, then speeds up and then becomes "
slow again.
.n
r
. Check the amount of.oxygen released at the steepesl part of the curve.
.'g
{
m . The S-shaped curve of the oxygen dissociation curve represents a particular
n
ffi property of haemoglobin called cooperativity.
. The steepest part of the curve shows that a slight drop in partial pressure of oxygen
can cause a large drop in the percentage of oxygen saturation of haemoglobin.
. The binding of the first oxygen molecule to one subunit of a haemoglobin
facilitates the others to change shape and increase their affinity for oxygen.
. In the same way, when one subunit releases or unloads its oxygen, the other three
undergo changes in their shapes and all the other oxygen molecules are released as well.
. When oxygen concentration drops; for example in respiring tissues, oxyhaemoglobin
responses by releasing more oxygen to be used by the respiring tissues.

Draw a directly proportional straight line through the origin on the following
oxygen dissociation curve. Compare the efficiency of oxygen released by
oxyhaemoglobin for both curves.

c
100
bo
s)80
E
o
cou
o
c
c40
-
=
o

I Stratasy
Compare the percentage of oxygeri released by both curves at a few particular points of Po2,
 Gaseous Exchange and lts Control 87

. ":
i.--* -*-,e$le-eg$gs-o-i$-grt-,-
.
I A small drop in the partial pressure
-- " i'. Ont.---9rylslllillEl*er_sry9 of_ _,
drop in the partial pressure j
,
: of oxygen causes a large drop in the oxygen causes a proportionate drop in
percentage ofoxygen saluration of ' the percentage ol'oxygen saluration of
;

haemoglobin. haemoglobin.

I . As a result, the oxygen released by I . As a result, the oxygen released by j

joxyhaemoglobinisenoughtosupportioxyhaemoglobinisnotenoughto
respiring tittr:r. . supqor.r respiring rissues.

Why does the oxygen dissociation curve of myoglobin shift to the left of the curve
for haemoglobin?
. Myoglobin shows a greater affinity for oxygen compared to haemoglobin.
Myoglobin only releases oxygen when partial pressure of oxygen is below 20 mmHg
or when supplies of oxyhaemoglobin is exhausted or finished.
This allows myoglobin to act as an oxygen store in resting muscles.

Explain why the curve of myoglobin is hyperbolic but the curve of haemoglobin
is sigmoidal.
. Myoglobin does not show cooperativity.
. o--:
:I
Haemoglobin shows cooperativity, that is, the binding of an oxygen molecule to one i>
,t
subunit induces the other subunits to change shape, thus increasing their affinity for -*t
m'
7
oxygen. nxffi
,# What will happen to the oxygen dissociation curve of haemoglobin if the pH of
the blood decreases? Explain.
. The curve is shifted to the right.
' The increase in the acidity of the blood is due to an increase in the concentration of COr.
' Haemoglobin releases oxygen more readily when the concentration of carbon
dioxide is high in order to supply enough oxygen to actively respiring tissues.

,# Explain why human haemoglobin becomes saturated with oxygen in the lung and
releases oxygen when it reaches the tissues.

# ' The high partial pressure of oxygen in lungs causes haemoglobin to pick up oxygen
readily (high affinity towards oxygen) to form oxyhaemoglobin.
' Low partial pressure of oxygen in tissues, due to respiring cells using oxygen
continuously, causes oxyhaemoglobin to dissociate and release oxygen to the
respiring tissues.

Explain the effect of carbon dioxide on an oxygen dissociation curve.

;ffi
a Carbon dioxide causes the Bohr effect.
a The higher the concentration of carbon dioxide, the more the oxygen dissociation
curve shifts to the right.
At high concentrations of carbon dioxide (high concentrations of H* or low pH), the
affinity of haemoglobin towards oxygen becomes less.
As a result, oxyhaemoglobin dissociates to release oxygen.
88 Gaseous Exchange and lts Control

-
The freed haemoglobin combines with H* and acts as a buffer to prevent acidity in
the red blood cell.
The oxygen released is used by the active respiring tissues.

Explain the effect of temperature on the oxygen dissociation curve of haemoglobin.

W
. An increase in temperature is associated with an increase in muscle or tissue activity.
. The heat generated lowers the affinity of haemoglobin for oxygen.
. The oxyhaemoglobin dissociates more to release oxygen to the active muscles or tissues.
. The oxygen dissociation curve is displaced to the right.

7.2 Role of Chemoreceptors in Controlling Breathing

Name the chemoreceptors which control or affect the breathing centre.
W

a Central chemoreceptor in medulla

a Peripheral chemoreceptor: aortic bodies and carotid bodies

01&
ry What is the role of the chemoreceptor?
.
# To detect drops in oxygen level or increase in carbon dioxide level or acidity in blood

lnspliati:n(!lgsilJratel
*---l
i-. Contraction ol
Stretch receptors in lncrease in CO2
diaphragm and outer
lungs stimulated paftial pressure in
intercostal muscles
blood detected by
I
I chemoreceptors
I
I
I stimulates
I
I
I no inhibitorv

no impulses
----_-----l
*
Relaxation of
Stretch receptors in
diaphragm and outer
lungs not stimulated
intercostal muscles
A -i'
I I
I________* Expiration (lungs deflate) .<--------r
 Gaseous Exchange and lts Control 89

Ql1S Explain what happens to intercostal muscles' ribcage and diaphragm during
=w inspiration and expiration.

# . During inspiration, the extemal intercostal muscles contract.

. The ribcage moves upwards and outwards.
. The diaphragm contracts, moves downwards and becomes flattened.
. Thoracic volume increases and the air pressure becomes lower than the
atmospheric pressure; air is drawn in.
. During expiration, the internal intercostal muscles contract.
. The ribcage moves downwards and inwards.
. The diaphragm relaxes, moves upwards and becomes dome-shaped.
. Thoracic volume decreases and the air pressure becomes higher compared to
atmospheric pressure; air is forced out of the lungs.

7.3 Gaseous Exchange and Control in Plants

Statetwo functions ofthe stoma.

&W
. Controls the rate of transpiration -n:..r1
. Controls the rate of gasbous exchange ?.. a--
>':.:.-
-tr t..'
"{ : :1.
m:.

ffi
Explain the regulation of stomatal opening based on the starch-sugar hypothesis.
@#
I n,nt
, The.higher thF amount o{ solute dissolved in a solutisn, the more negative its waier
Botential betomes.

During daytime, carbon dioxide is used in photosynthesis.

Photosynthesis produces glucose that is soluble in the guard cells.
The accumulation of sugars will lower the water potential; that is, water potential
becomes more negative in the guard cells.
Water from the subsidiary cells will enter the guard cells by osmosis.
The guard cells become turgid.
Turgor pressure in the guard cell causes its thin and flexible outer cell wall
(bordering subsidiary cells) to be more stretched compared to the thicker and less
flexible inner cell wall (bordering the stomatal opening).
a As a result, an oval-shaped opening is formed between the guard cells.

Explain the regulation of stomatal closing based on the starch-sugar hypothesis.

W
At night, glucose is converted into starch in the guard cells.
Starch is osmotically inactive.
As a result, the water potential of the guard cells increases and becomes higher than
that of the surrounding subsidiary cells.
o Water leaves the guard cells by osmosis.
a This decreases the turgidity of guard cells, leading to the stoma closing.
 90 Gaseous Exchange and lts Control

OBJECTIVE OUESTIONS

7.1 Gaseous Exchange and C II and III only

Control in Mammals D I, II and III

I Which of the following features are 3 From the figure, what is the percentage
required for gaseous exchange? of oxygen released by human
I Moisture haemoglobin at 40 mmHg partial
II Pressure gradients pressure of oxygen?
III Transport proteins A 907o C 45Va
A I only B 547o D 827o
B I and II only
C IIandIIIonly Which of the following statements is not
D I,IIandIII true?
A Haemoglobin can act as a buffer.
B Haemoglobin binds loosely and
Questions 2 and 3 refer to the.figure below.
reversibly to oxygen.
C Haemoglobin consists of four
polypeptide chains.
100
D Haemoglobin can bind with two
.c 90
!
o
molecules of oxygen.
o 80
o
E 70
o
(g Most of the carbon dioxide produced by
c 60
o the body tissues is transported to the lungs
c 50
o
g
in the form of
40
f
($ A carbonic acid
a 30
B bloodplasma
20
C carbaminohaemoglobin
10
D bicarbonate ions
20 40 60 80 100
Partial pressure of oxygen (mmHg) Which of the following is true about
Haemoglobin of organism X haemoglobin?
- Human haemoglobin A Haemoglobin combines with oxygen
at high partial pressures ofcarbon
The figure above shows the oxygen dioxide.
dissociation curves of haemoglobin in B Haemoglobin combines with oxygen
organism X which lives in the human when the pH of the blood drops.
intestine, and human haemoglobin. C Haemoglobin releases oxygen when
I The haemoglobin of organism X has the temperature is lower.
greater affinity for oxygen. D Haemoglobin releases oxygen more
II The haemoglobin of organismXcan readily in highly active tissues.
get oxygen from human
haemoglobin. The following reaction shows the
III Human haemoglobin can be affinity of haemoglobin towards oxygen
saturated with oxygen at low partial in animal tissues under conditions
oxygen pressures. XandY.
A I only Y
---.
Hb + 40, HbOs
B IandIIonly Y
 Gaseous Exchange and lts Control 91

Which of the following represents III X is the oxygen dissociation curve

conditions X andY? at a partial pressure of carbon
dioxide that is higher than that for IZ
i ,X ..'* I Y i
A I only
High partial Low parrial B I and II only
pressure ol O, : pressure o1'CO, C II and III only
u:^L pafiial
High -^-:^t I
rr:^r partial
High -^*:^t
i
D I, II and III
pressure of O, pressure olCO, j
j Y-l ::i-::-:-'-*"-:?-*-- l0 to 12 refer to the graph below.
Questions
C Low partial High partial
i,Pl-".Ty-1.,or9-,-- i PryFgle- if 9-o_a i
10 The graph below shows the oxygen
dissociation curve of haemoglobin. X, Y
D High r Low hydrogen ion
and Z represent three different locations
]9ry=tu::--* ic91:-ell11"-l- * - inside the body. Choose the correct
Which of the foliowing is true about location forX,Y andZ.
the oxygen dissociation curve of G 100
haemoglobin? ;o
A It shows the effect of carbon dioxide o80
o
o
on the curve. E

B It is a curve showing the percentage c3oo

o
saturation of haemoglobin with c
.9 40
oxygen at different partial p{essures 6
-
ofoxygen. Szo
C The X axis on the graph shows o
the percentage saturation of
20 40 60 80
haemoglobin with oxygen.
(7o HbO3).
ttl
XYZ
100

Partial oxygen pressure (mmHg)

D The Yaxis shows concentrations of
oxygen as partial pressures.
i X, .t*-*l***-*-*----i**-*---**-
j,, t'I"t,'t'.:1,::; Z : ,j

Which of the following statements is Lungs j Tissues Tissues

true about the oxygen dissociation during
i at rest
curves X and Y shown below?
i Tissues during Lurrg5
rlssutrbuurrlB ; Lungs : Tirru.t
rrssucs :

6 100
exercise i iatrest
dt lcs:
c
.,tl-*.t:---"-* -,---*-:-*-- -*-
:
i ]I
o
o C : Tissuesduring'Tissues Lungs
o
c i exercise i at rest ; i

=
c -^
o5U
D Tissues Lungs Tissues '
F
6
f
i atrest : i during i

6
r -- :
g
o
E
.9
tI-
11
--
What are the percentages of haemoglobin
--i-:ryr!s i

U saturated with oxygen atX,Y andZ?

50 100 -r---" '..-"::T:-*T-'-
Partial oxygen pressure ,x:,Yzt -:-*..-. . -.
ti 2i!: - -,- 991'- - r- --?t?-
30% 1 toEo i =*****-*.l
:

At P, there is more oxygen in X than B;i---*---=-:*:*|*-*---*--_*-+-- soqo i

that in Y.
At P, oxygen is released much easier
c -M:- : *: ::l: --.*-89L- -.;

by lthan by X. l87o
f):i-***-*---- r
70Vo 98Vo
L*-_*-_*-_-j
:

-*----***-
 92 Gaseous Exchange and lts Control

12 What are the percentages of oxygen II Carbon dioxide can bind to the
readily released atX andY? amino group of haemoglobin.
III Carbon dioxide combines with water
to form carboxylic acid.
A I only C II and III only
B I and II only D I, II and III
16 The acidity due to the accumulation of
H* in red blood cells is buffered by
A haemoglobin
13 The graph below shows the effect of pH B plasma proteins
(X, Y and Q on the oxygen dissociation C carbon dioxide
curve of haemoglobin. Match the curves D oxygen
with the correct pH.
7.2 Role of Chemoreceptors
in Controlling Breathing
.E
5€
Oo
ao 17 Which of the following statements is
XE true?
iF
g;
oo
A The breathing rate is completely
Ec^ 40 under voluntary control.
'1 i] f.1.
.,
--t_! : :r
-:-ll:- f:-
B The chemoreceptors are located on
,,.'.,. T r€ en
-.. : m the diaphragm and intercostal muscle.

ro :.)o

0
20 40 60 80 100
C During expiration, the external
intercostal muscles and diaphragm
P^
v2
(mmHo) contract.
D CO2 released from respiration is
detected by chemoreceptors in the
carotid and aortic bodies of the blood
system.

18 The flow charl below shows a series of

mechanisms involved in breathing.
Determine the structuresX.Y andZ.

14 Which of the following statements is not

true about myoglobin?
A Myoglobin can be found in skeletal
muscles.
B Myoglobin shows high affinity
towards oxygen.
-'**l--_ -------
C Myoglobin consists of two !, X il- -
Y 'r,- :2":'.1
--1
polypeptide chains. A Baroreceptor Intercostal Diaphragm :

D Myoglobin can only bind to one * muscle

r
--,* --.*'*- i
oxygen molecule. B rChemoreceptor iDiaphragm ilntercostal j

15 Which of the following statements is

, - - -- - -i ---- rulgle--- -- i

C Diaphragm .Chemoreceptor Intercostal

true? 1- _ *i_ __ _ * -!pl991e j

I Carbon dioxide dissolves in the D Stretch receptor Diaphragm Intercostal

i
j
:
i

blood plasma. t----,-.-,-,-,--*--,i-*- -** *---*-*qu:i1..*

-i
 Gaseous Exchange and lts Control 93

t9 The diagram below shows structure 20 The figure shows the structure of guard
R. Structure S which is located in the cells in two different conditions, P and
wall of structure R is able to control 0. Which of the following statements
inspiration by sending inhibitory are true?
impulses to the respiratory centre. I The water potential of the guard
What are structures R and,S? cells is higher in P than in Q.
II Sugar accumulates in P.
III Water moves out from the guard
cells by osmosis in B.
A I only
B I and II only
C II and III only
D I, II andIII
i.:YY"*ffi]Y'--:'l-Y:
RSi
*---j^"-''."-.-'"-.^'^"--*--
21 Which of the following causes
A -_ Traghgg . j_ury!.c*epgi the guard cells to change shape
n l-*irq*Ir'-- -i* -clssgtgeqJe:* j from P lo Q?
A Increase in the water potential of the
C ;_ Jryggli_ _ _S11e1ch
receptor_
guard cells
D Alveoli : ChemorecePtor
- L--,,* B Outward movement of water by
osmosis from the guard cells
7.3 Gaseous Exchange and C Accumulation of glucose in the
.n
1.-
ts ..
Control in Plants guard cells {.,
3
n'
x.
Questions 20 to 2l are based on the figure D Outward movement of glucose from ffi
below. the guard cells

,
. . ,: ...:...,..:',
i :: , ., 3 ..Xf :.. r F,:g[ .,..,:..:] .6I ..:' .d[::8I q iI
:,': ',..11:
': V' 9]f $:'$t: )rfI. YgI acT {III' 3SI S5
ir..-r. . :-"lf{-l tg. €[ l: :" :d:..g ',t,,..(I,,8,. .':Q?.:, ]f g"7 tt I
94 Gaseous Exchange and lts Control

.CI{AITENG E'(}U ESTIONS

Structured Ouestions
1 The diagram below shows gaseous exchange that takes place between erythrocytes and
respiring tissues.
/*"pirin)
tissue
O^- X
\' /,/

blood
1,6
/f
I/I
J I
/ -..'--" \
X-H.O--Y:H,Z
I *+n^c
I NaHC03
capillaryl (or.-HbHbOs -+ Hb " HHb
4O2*
NaCl
II \---l
\ -r---\
red blood cell
-,/
process A'Cl-

(a) State two ways in which carbon dioxide is transported in blood.

(2 marks)

(b) Name the gas labelled X and substances labelled Y and Z.

(3 marks)

(c) What is process A? State its function.

(2 marks.l

(d) Based on the diagram, explain the function of haemoglobin.

(1 mark)

(e) Based on question (d), state another substance found in blood which has the same
lunction as haemoglobin.

(1 mark)
 Gaseous Exchange and lts Control 95

The graph below shows oxygen dissociation curves at three different partial pressures of
carbon dioxide, P.o, represented by curves P, Q and R.

20 40 60 80 100
X
(a) Label axesXand L

(1 mark)
(b) Give the name of the effect of carbon dioxide on the oxygen dissociation curve.

(1 mark)

(c) Based on the graph shown,

(i) what are the percentagbs of oxyhaemoglobin for the oxygen dissociation curves P,
Q and R at 30 mmHg partial pressure of oxygen?

(3 marks)

(ii) calculate the amount of oxygen being used by tissues for oxygen dissociation
curves P, Q and R at 30 mmHg.

(3 marks)

(d) What happens to the oxygen dissociation curves when the partial pressure of carbon
dioxide increases? Explain your answer.

(2 marks)

Essay Q,uestions
1 (a) What is meant by Bohr effect? Explain how Bohr effect occurs and its effect on active
tissues. (10 marks)
(b) Explain the oxygen dissociation curve of haemoglobin. (10 marks)

2 Explain the role of chemoreceptors in controlling the rate of breathing in the human
respiratory centre. (20 marks)
96 Gaseous Exchange and lts Control

Structured Questions . In the presence of high concentrations of

H* (more carbon dioxide present) or low
1 (a) . As hydrogen carbonate ions in the
pH, haemoglobin acts as a buffer.
red blood cells .
. HbO, dissociates into oxygen and
Combined with the amino group of
haemoglobin and the freed haemoglobin
haemoglobin to fbrm
combined with H* to form haemoslobinic
carbaminohaemoglobin
. Dissolved and transported in blood acid.

plasma as carbonic acid HbO, -+ Hb + 40,

(Any two) J <- H* from
(b) X: carbon dioxide I: carbonic acid HHb carbonic acid
Z: bicarbonate ion/hydrogen carbonate ion (haemoglobinic acid)
(c) Chloride shift
. Therefore, in active tissues with higher
Function: Maintains the electrochemical carbon dioxide levels, haemoglobin
neufrality or charge balance ofred blood releases oxygen readily to supply enough
cells oxygen to the tissues.
(d) Haemoglobin acts as a buffer to prevent (b) . The oxygen dissociation curve of
blood from becoming acidic. haemoglobin is a curve that shows the
(e) Albumin, one of the plasma proteins percentage of oxygen saturation of
haemoglobin at different partial pressures
2 (a) X: partial pressure of oxygen (mmHg) ofthe oxygen.
)/: percentage of haemoglobin saturated
. The .r-axis of the graph shows the
with oxygen concentration ofoxygen as partial pressure.
(b) Bohr effect
. The)-axis shows the saturation
(c) (i) P: 65Va, Q: 50Vo, R: 40Va percentage of the haemoglobin with
(ri) P: 99198 - 65 = 34/33Vo oxygen.
. When the oxygen concentration is
Q:97 /96 - 50 = 47l46%a
R:96/94-40=56/547o very low, the percentage of saturation
(d) . The oxygen dissociation curves are with oxygen is also very low.
displaced to the right.
. As thepartial pressureofoxygen
. The higher the carbon dioxide level, the increases, the curve starts to rise rapidly
more oxyhaemoglobin dissociates to until saturation reaches maximum.
release oxygen to active tissues.
. The S-shaped graph shows that a very
small change in the partial pressure
oxygen causes a big drop in the saturation
Essay Questions of the haemoglobin with oxygen.
I (a) . Bohreffectistheeffectofrhe . This means that as the blood enters the
concentration of carbon dioxide in blood Iungs, it is rapidly saturated with oxygen
on the affinity of haemoglobin towards but a small drop in the oxygen level at the
oxygen. respiring tissues will cause a lot of
. Carbon dioxide reduces the affinity of oxygen to be dissociated from the
haemoglobin towards oxygen and haemoglobin.
therefbre shifts the oxygen dissociation .
2 Carbon dioxide that is released from
cufve to the dght.
. respiration into blood lowers the blood pH and
Carbon dioxide produced by respiration
this change is detected by chemoreceptors in
reacts with wateq forming carbonic acid.
. the carotid and aorlic bodies ofthe blood
This reaction is catalysedby carbonic
system.
anhydrase.
. The impulses generated are sent to the
carbonic anhydrase
CO, + HrO inspiratory centre in the medulla.
H2COI
. From the inspiratory centre, the impulses are
Carbonic acid dissociates into hydrogen
sent to the external intercostal muscles via the
ion and hydrogen carbonate ions.
intercostal nerve and diaphragm via phrenic
H,CO.:11*+HCO. nerve.
 Gaseous Exchange and lts Control 97

The extemal intercostal muscles and
diaphragm contract and enable air to enter the
lungs.
Inspiration takes place.
When the lungs expand, the stretch receptors
within the walls of the alveoli and bronchioles
are stimulated.
Inhibitory impulses are sent to the expiratory
centre, which automatically cuts off
inspiratory activity.
The extemal intercostal muscle and diaphragm
relax.
Air is forced out ofthe lung and expiration
takes place.