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Objective:

describe the structure of red blood cells, phagocytes and lymphocyt


the role of haemoglobin

Composition of blood-
Whole blood

55% plasma

10% solutes

90% water

45% cells

red

white

platelets

nutrients
agranulocytes

granulocytes

salts (electrolytes)
eosinophils
hormones

monocytes

lymphocytes

basophils
plasma proteins
T cells
albumens
globulins (antibodies)
clotting factors

killer T
cells

helper
T cells

B cells

neutrophils

Blood cells
Platelets
Neutrophil
Monocyte

Red blood cell

T-lymphocyte
False colour scanning electron micrograph of cells
in arterial blood

Red blood cells (erythrocytes)


5 000 000 3


7
, 2
(
)
,
(100-120 )
;
(1-2
/ )

Objectives:
* describe the role of haemoglobin in carrying oxygen and carbon dioxide
** describe and explain the significance of the dissociation curves of adult
oxyhaemoglobin at different carbon dioxide levels (the Bohr effect)
:
*

**

( )

Haemoglobin and oxygen transport-

Haemoglobin is a conjugated protein showing quaternary structure


One haemoglobin molecule is formed of two a-globin and two b-globin
chains, each bonded to a haem group with an iron atom at its centre

- -,

a-globin
b-globin
haem

Haemoglobin and oxygen transport

Each haem group can bind one oxygen molecule (O2) to its iron atom: one haemoglobin
molecule can therefore carry four oxygen molecules
Unbound haemoglobin has quite a low affinity for oxygen, and at low oxygen concentrations
(as in respiring tissues) very little is bound
But the binding of an oxygen molecule to one haem group alters the shape of the whole
molecule, making it easier for a second to bind; this alters the shape making it easier for a
third to bind, and so on: this gives the characteristic oxygen dissociation curve of
haemoglobin
(O2)
:
,
(, )

, ;
:

Oxygen dissociation curve of haemoglobin


100

Percentage
saturation of
haemoglobin
with oxygen

An oxygen dissociation curve plots the percentage saturation of


haemoglobin with oxygen against the partial pressure of oxygen in its
surroundings.
Percentage saturation is a measure of how full up the haemoglobin is with
oxygen: if none of the haem groups are bound to oxygen, saturation = 0%; if
all of them are bound, saturation = 100%; if on average each haemoglobin
molecule has two oxygen molecules bound to it, saturation = 50%, and so
on.

50


.
, ""
: ,
= 0%, , = 100%,

, , = 50%, .

0
Partial pressure of oxygen (pO2) / kPa

(2) /

Oxygen dissociation curve of haemoglobin-



100

Percentage
saturation of
haemoglobin with
oxygen

Partial pressure of oxygen is a measure of oxygen concentration that


allows direct comparison between, for example, oxygen concentration in the
air, oxygen concentration when dissolved in water, or oxygen concentration
when bound to haemoglobin.
Other concentration measures (e.g. %, or mg per dm 3, or whatever) would
not allow such comparison.

50


, ,
, ,

.
(,%, 3,
) .

0
Partial pressure of oxygen (pO2) / kPa

(2) /

Oxygen dissociation curve of haemoglobin-



100

Partial pressure of a gas in a mixture of gases is the part of the total pressure
of the mixture that is exerted by that gas alone.
E.g. if total atmospheric pressure is 100 kPa, and oxygen makes up 20.7% of
the atmosphere, than the pO2 in the atmosphere is 20.7kPa.

Percentage
saturation of
haemoglobin with
oxygen

If a mixture of gases in a cylinder exerts a total pressure of 2000 kPa, and


oxygen makes up 40% of the mixture, what is the pO2 in the cylinder?

50


, , .
100
20,7% , 2 20.7kPa.
2000
40% , 2 ?

800 kPa

0
Partial pressure of oxygen (pO2) / kPa

(2) /

Oxygen dissociation curve of


haemoglobin
100

Percentage
saturation of
haemoglobin 50
with oxygen

Partial pressure of a gas in a solution or bound state is equal to the partial


pressure of that gas in an atmosphere in equilibrium with that solution.
E.g. if a body of water is in equilibrium with an atmosphere of pO 2 20.7 kPa,
so that oxygen is being neither gained nor lost by the water, then the pO 2 of
the water is also 20.7 kPa.
If a test-tube full of blood is in equilibrium with an atmosphere of pO 2 12.5
kPa, then the pO2 of the blood is also.


.
2 20,7
, , ,
2 20,7 .
pO2
12,5 , 2 ..........

12.5 kPa
Partial pressure of oxygen (pO2) / kPa

Oxygen dissociation curve of


haemoglobin
Tissue pO2

Alveolar pO2

100

Percentage
saturation of
haemoglobin 50
with oxygen

0
0

As pO2 continues to rise, percent


saturation rises increasingly steeply
pO2 of exercising
as
affinity
for
At the
pO2haemoglobins
0 kPa (no oxygen
present)
muscle
oxygen
percentincreases
saturation is of course 0
Above a pO2 of about 8 kPa
As pO2 rises from
0,ofso
percent
most
thedoes
haem groups
are bound toof
oxygen,
saturation: but because
the and
the curve flattens out.
increasing affinity of haemoglobin
2 8
for oxygen as each
O2
molecule

but
binds, the curve,
is not
linear
,
increases in gradient
.

2
4
6
8 10
12
14
Partial pressure of oxygen (pO2) / kPa

Oxygen dissociation curve of haemoglobin:


why is it important?- ?
Tissue pO2

Alveolar pO2

100

Percentage
saturation of
haemoglobin 50
with oxygen
Compare the oxygen
dissociation curve to the curve
we would see if haemoglobin
reached saturation at the same
pO2 but without the increasing
affinity.


,

pO2
.

pO2 of exercising
muscle

The sigmoid dissociation curve means


that at low pO2 haemoglobin binds
oxygen less readily than expected i.e.
lets it go more readily than expected.
The extra oxygen delivered is shown by

,
pO2
,
-
, .

0
0

2
4
6
8 10
12
14
Partial pressure of oxygen (pO2) / kPa

Oxygen dissociation curve of haemoglobin: fetal haemoglobin


Placental pO2

Alveolar pO2
At the placenta, fetal haemoglobin must load
(take up oxygen) at a pO2 at which maternal
haemoglobin unloads.

100

Percentage
Fetal
saturation of
haemoglobin
haemoglobin 50
with oxygen

This means that fetal haemoglobin must have


a higher affinity for oxygen than maternal
haemoglobin: its dissociation curve is
therefore to the left of maternal haemoglobins
curve.

Maternal
haemoglobin

,
( )
2,
.
,

, :

.

Fetal haemoglobin is made


in the liver.
Why not in bone marrow,
like adult haemoglobin?

.

,
?

0
0

2
4
6
8 10
12
14
Partial pressure of oxygen (pO2) / kPa

Oxygen delivered from


maternal to fetal
haemoglobin

Oxygen dissociation curve of myoglobin-



Tissue pO2

Alveolar pO2

100
Myoglobin
Percentage
saturation of
haemoglobin 50
with oxygen

pO2 of exercising
muscle

Adult
haemoglobin

As the curve shows, myoglobin


gives up most of its oxygen only
when muscle pO2 falls well below
1 kPa only in conditions of
severe exertion.
Next stop, anaerobic respiration
,


, 2
1 -
.
,
...

0
0

2
4
6
8 10
12
14
Partial pressure of oxygen (pO2) / kPa

Myoglobin is a dark red pigment


found only in muscle. It acts as a
last-ditch oxygen reserve in severe
exertion: its oxygen dissociation
curve is a long way to the left of
haemoglobins.

.
"
'
:

.

Transport of carbon dioxide



About 5% of the carbon dioxide released from respiring cells is
carried as CO2 molecules in solution in blood plasma
About 25% attaches to the protein in haemoglobin and is carried as
carbaminohaemoglobin

5%
2,

25%
carbaminohaemoglobin

Transport of carbon dioxide-

The remaining 70% enters red blood cells and is converted by the enzyme
carbonic anhydrase into carbonic acid
The carbonic acid immediately dissociates into hydrogen ions and
hydrogencarbonate ions:
70%


:

CO2 + H2O

H2CO3

H+ + HCO3-

The hydrogencarbonate ions diffuse out into the plasma: the loss of negative ions is
balanced by a corresponding uptake of chloride ions, Cl- (the chloride shift)
:
, Cl-(
)

Describe and explain the significance of the increase in


the red blood cell count of humans at high altitude;
Describe how smoking can affect oxygen di


;
,
ssociation curve

Transport of carbon dioxide-

The diagram represents a red blood cell with oxygen-saturated haemoglobin, arriving at a respiring
tissue with a high CO2 concentration
,
CO2

CO2

The H+ ions combine with haem groups to form haemoglobinic


acid
+
haemoglobinic ...

CO2 + H2O
Carbonic
anhydrase

H2CO3

H+
HCO3-

O2
O2 H + O 2
O2
Haemoglobinic
acid

HCO3- ClThe chloride shift

Transport of carbon dioxide


The diagram represents a red blood cell with oxygen-saturated haemoglobin,
arriving at a respiring tissue with a high CO2 concentration
Haemoglobinic acid not only buffers the
excess H+ ions, but its lower affinity for
oxygen causes O2 to be released

CO2

CO2 + H2O
Carbonic
anhydrase

H2CO3
In the alveolar capillaries the opposite
happens: the high O2 concentration
displaces H+ from haemoglobin; the H+
ions combine with HCO3- to form
carbonic acid, which decomposes to
CO2 and water.

H+
HCO3-

4O2

H+
Haemoglobinic
acid

HCO3- ClThe chloride shift

The formation of haemoglobinic acid means that in the presence of high


CO2 concentrations the dissociation curve shifts to the right (a
reduction in affinity for oxygen): this is called the Bohr effect.

The Bohr effect

haemoglobinic ,
2
( ): .

100

Percentage
saturation of
haemoglobin 50
with oxygen

Loading occurs here

Low CO2
level

High CO2
level
Medium CO2
level

Unloading
occurs here

0
0

The Bohr effect means that haemoglobin


will load more easily in the pulmonary
capillaries (low CO2 = high O2 affinity),
and unload more easily in the tissue
capillaries (high CO2 = lower O2 affinity).
,

( 2 =
O2 ),
(
CO2 O2 = ).

2
4
6
8 10
12
14
Partial pressure of oxygen (pO2) / kPa

Oxygen dissociation curves: practice questions- :


Loading tension is defined as the


partial pressure of oxygen (pO2) at
which haemoglobin becomes 95%
saturated; unloading tension is the
pO2 at which haemoglobin becomes
50% saturated.
State the loading and unloading
tensions of the haemoglobin in the
red curve.


(2),

95% ;
2,
50%
.

% saturation

Partial pressure of oxygen (pO2) / kPa

Oxygen dissociation curves: practice questions-


:
2
Calculate the volume of oxygen
delivered by 1 dm3 of blood when
travelling from the alveoli (pO2 12
kPa) to the liver (pO2 4.6 kPa).
1 3
200 3
.
,
1 3

(2 12 ), (2 4,6
).

% saturation

1 dm3 of human blood can carry 200


cm3 of oxygen when fully saturated.

Partial pressure of oxygen (pO2) / kPa

Oxygen dissociation curves: practice


questions
3

Llamas are herbivorous mammals


living high in the Andes, where the
atmospheric pO2 is much lower than
at sea level. Where would the
oxygen dissociation curve of llama
haemoglobin appear on this graph?
Explain your answer.


.

% saturation

The red line shows the oxygen


dissociation curve of adult human
haemoglobin.

Llama
haemoglobin
Human
haemoglobin


,
,
pO2 ,
.


?
.

Partial pressure of oxygen (pO2) / kPa

Oxygen dissociation curves: practice


questions
4

Where on this graph would you


expect to see (a) the oxygen
dissociation curve of human fetal
haemo-globin at pCO2 0.1 kPa, (b)
the oxygen dissociation curve of
adult haemoglobin at pCO2 of 0.2
kPa? Explain your answers.



2 0,1 .

% saturation

The red line shows the oxygen


dissociation curve of adult human
haemoglobin at pCO2 of 0.1 kPa.

Fetal
haemoglobin
at pCO2 0.1
kPa
Adult
haemoglobin
at pCO2 0.2
kPa


()
2 0,1 , ()

2
0,2 ? .

Partial pressure of oxygen (pO2) / kPa

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