Adaptations for Transport
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Transcript of Adaptations for Transport
Adaptations for Transport
GCE BIOLOGYBY2 Adaptations for Transport Next The haem part of the
molecule contains iron.
Click on the magnifying glass to enlarge this image of the
haemoglobin molecule + The haem part of the molecule contains iron.
Each molecule has four haem groups and each one of these can bind
with an oxygen molecule. Hb + 4O HbO8 Next Oxygen Dissociation
Curve
Click the numbered sections on the graph for an explanation of what
happens at each stage Oxygen Dissociation Curve Saturation of
Haemoglobin / % Partial Pressure of Oxygen/ kPa 2 4 6 8 10 12 20 40
60 80 100 3 ? 2 A small change in partial pressure of oxygen
results in a large change in percentage saturation. At high partial
pressures of oxygen the Hb has a high percentage saturation and
therefore has a high affinity for O2. At low partial pressures of
Oxygen the Hb has a low percentage saturation and therefore has a
low affinity for O2. Show/ hide titles Show/ hide scale Show/ hide
line 1 Next ? O2 O2 Haemoglobin This diagram shows how a model of
haemoglobin reaches saturation with oxygen. haemoglobin The
molecule is now saturated. Back O2 O2 HIGHER PRESSURE (kPa) Click
on the above boxes to see movement of the molecules. The oxygen
partial pressure (pO2) is a measure of oxygen concentration. The
higher the concentration of dissolved oxygen, the higher the
pressure. Back Oxygen Dissociation Curve
100 80 60 Saturation of Haemoglobin / % 40 Samples of haemoglobin
can be placed in different partial pressures of oxygen, before
estimating how much of it becomes bound to the oxygen. We can plot
the percentage saturation againstthe partial pressure to get an
oxygen dissociation curve. 20 Show/ hide line 2 4 6 8 10 12 Next
Partial Pressure of Oxygen/ kPa Incorrect Correct The haemoglobin
is almost saturated at a high partial pressure of oxygen A molecule
of haemoglobin can carry seven molecules of oxygen at most
Oxyhaemoglobin dissociates at a low partial pressure of oxygen The
group haem contains iron Respiring tissues have a high partial
pressure of oxygen Next Note that each haemoglobin molecule
contains four haem groups
Why is an Oxygen Dissociation Curve S-shaped? Hint Answer 100 80 60
Note that each haemoglobin molecule contains four haemgroups
Saturation of Haemoglobin / % 40 When the first oxygen molecules
binds to the first haem group, the haemoglobin molecule loses its
shape. This makes it easier for the three other molecules to
combine with the remaining haem groups. 20 2 4 6 8 10 12 Next
Partial Pressure of Oxygen/ kPa The Effect of CO2 on the Oxygen
Dissociation Curve
How much oxygen is transported by a molecule of haemoglobin also
depends on partial pressure of carbon dioxide. 2 4 6 8 10 12 20 40
60 80 100 Show hide CO2 line CO2 Saturation of Haemoglobin / % From
the graph we see that at high partial pressures of carbon dioxide,
the oxygen dissociation curve shifts to the right. This is called
Bohrs shift. Higher partial pressure of carbon dioxide increases
the dissociation of oxyhaemoglobin. Next Partial Pressure of
Oxygen/ kPa The Effect of CO2 on the Oxygen Dissociation
Curve
What is the significance of this in the body? Answer 2 4 6 8 10 12
20 40 60 80 100 CO2 Saturation of Haemoglobin / % When
oxyhaemoglobin reaches the tissues, the high partial pressure of
carbon dioxide from respiration causes oxyhaemoglobin to release
its oxygen more easily. So oxygen is released where its needed.
Next Partial Pressure of Oxygen/ kPa The Effect of pH on the Oxygen
Dissociation Curve
2 4 6 8 10 12 20 40 60 80 100 pH CO2 Saturation of Haemoglobin / %
Show/ hide the pH curve Show/ hide the CO2 curve Next Partial
Pressure of Oxygen/ kPa Explain what you see here
(Keep in mind what youve already seen) HINTS What happens to the
level of CO2 in the water? What has happened to reduce the pH of
the water? pH What does the pH meter show? What has happened to the
level of oxygen in the water? Next Discuss each image in turn what
do they have to do with oxygen dissociation?
Next The Oxygen Dissociation Curve of an Athlete in Training
2 4 6 8 10 12 20 40 60 80 100 The further left the curve shifts,
the easier it is for haemoglobin to pick up oxygen. Saturation of
Haemoglobin / % The further the oxygen dissociation curve shifts to
the right, the easier it is for the haemoglobin to give up its
oxygen. Next Partial Pressure of Oxygen/ kPa Haemoglobin Myoglobin
O2 O2 Found in the blood.
It joins to 4 molecules of oxygen at its maximum saturation but low
affinity compared to myoglobin. The haemoglobin never reaches 100%
oxygensaturation Found in tissues. It binds to only one molecule of
oxygen but there is greater affinity to oxygen. 3.The myoglobin can
reach 100% oxygen saturation. Next Oxygen Dissociation Curve for
MYOGLOBIN
2 4 6 8 10 12 20 40 60 80 100 Myoglobin Myoglobin is a molecule in
muscles that combines with oxygen. The oxygen dissociation curve
for myoglobin is far to the left of haemoglobin. What does this
mean? When is a person likely to obtain oxygen from the
dissociation of oxyhaemoglobin? Saturation of Haemoglobin / %
Haemoglobin Next Partial Pressure of Oxygen/ kPa Foetus What is the
function of the placenta? Answer placenta
The blood of the foetus and the mother flows closely together, but
never mixes. This allows substances like oxygento diffuse into the
blood of the developing foetus. Next Oxygen Dissociation Curve for
a Foetus
2 4 6 8 10 12 20 40 60 80 100 Foetal haemoglobin We see form this
graph of oxygen dissociation that foetus haemoglobin binds more
easily to oxygen than the mothers haemoglobin. Why is this higher
affinity advantageous to the foetus? Is there a disadvantage to the
mother? Saturation of Haemoglobin / % Mothers haemoglobin Show/
hide line Partial Pressure of Oxygen/ kPa