Transport of Oxygen and

Carbondioxide
 Transport of oxygen
From lungs to the tissues O2 is carried in blood in 2
forms:
1) Bound to Hemoglobin : 97%
2) Dissolved in plasma : 3%
1) O2 Dissolved in plasma
 Only 3% of total O2 is transported in
dissolved form.
 0.3ml of O2 /100ml of blood /100mmHg pO2

 This dissolved form determines PO 2 in blood &

hence regulates chemical regulation of resp.

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Oxygen Transport in the Blood

3%

97 %

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 2) O2 Combined with Hemoglobin

 97% of oxygen is transported in bound form with

Hemoglobin.
 Most of the O2 that diffuse into blood rapidly enter into
RBC and bind with Hb.
 Each Hb ,has 4 heme groups with Fe2+
 O2 bind with Fe2+
 One Hb molecule carries 4 O2 molecules.
 Hb bound with O2 is called oxy hemoglobin(HbO8)
 Oxygenation of hemoglobin is a reversible process
 When O2 is released from Hb it forms deoxy Hb(HHb)

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 Co-operative binding of O2 with Hb
 Binding of one molecule of oxygen in site of Hb
influences binding of other O2 molecules.
 As each O2 molecule bind with Hb ,the O2 affinity
increases progressively….+ve co-operative binding
 Oxygenation is a rapid process….<0.01sec

 Hb4 + O2 ↔ Hb4O2
 Hb4O2 + O2 ↔ Hb4O4
 Hb4O4 + O2 ↔ Hb4O6
 Hb4O6 + O2 ↔ Hb4O8

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 When fully saturated 1g of Hb can carry 1.34ml of O2
 So O2 carrying capacity of blood = 1.34 Χ Hb concn/100ml
= 1.34 X 15 = 20.1ml/dl

 In our body Hb is never saturated 100% because of

Physiological shunt
Ventilation –perfusion mismatch

 So in arterial blood
15 Χ 1.34 Χ 97/100 = 19.5 ml of O2 bound Hb /100ml

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Oxygen-hemoglobin dissociation curve
 O2 dissociation curve - ODC
 The O2 carrying capacity of Hb is given by oxygen Hb
dissociation curve.
 Graphical relationship between
 pO2 in X-axis and
 % saturation of Hb with O2 on Y-axis.
 Sigmoid shape- S shape ( as 1st molecule of O2 binds with
Hb slowly and the subsequent O2 molecules binds faster
than the previous one)
 The graph has 2 parts :
 Flat top :plateau phase – pO2 60-100 mmHg
 Steep fall : pO2 < 60 mmHg
 When pO2 is 100mmHg ,Hb is about 97% saturated .

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 Significance of flat top part
 When the pO2 of inspired air falls from 100 to 70 mmHg,
percentage saturation of Hb falls only from 97% to 92.5%
 O2 content of arterial blood falls from 20mL/dL to 18 mL/dL.
 This explains why people suffer less impairment in their
uptake of O2 at high altitude and in cardiorespiratory
diseases
 Significance of steep part
 When pO2 falls below 40mmHg, curve becomes steeper
causing more release of O2 from hemoglobin to prevent
tissues suffering from hypoxia.

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 P50
 The pO2 value at which Hb is 50% saturated with O2
 Normally P50 is 27 mmHg in adults.
 Significace of P50

 It is a convinient index to tell the hemoglobin affinity

for O2. Hemoglobin affinity for O2 is an inverse
function of P50 value ie:higher the P 50,the lower the
affinity of hemoglobin for O2.

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 Factors shifting curve to right & left
Shift of ODC to right ODC Shift to left
 O2 affinity of Hb will be  O2 affinity of Hb will be
less more
causes causes
 increase in  decrease in
Temperature Temperature
 increase in 2,3-DPG  decrease in 2,3-DPG
 increase in pCO2  decrease in pCO2
 increase in H+  decrease in H+
concentration concentration
 Carbonmonoxide
 Foetal Hb
 Myoglobin

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5. CO
6. Fetal Hb
7. Myoglobin

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 Shift to Left
 Affinity of Hb to combine with O2 increases, causing
less release of O2 to the tissues.
 Carbon monoxide shifts the curve to left due to
inhibition of synthesis of 2,3 DPG
 Fetal hemoglobin :Affinity of HbF for 2,3DPG is
considerably less than that of HbA. Therefore, HbF
shifts the curve to left.
 Myoglobin: it contains only one heme group with 1
atom of Fe . It takes up O2 at low pressure much
more readily. Thus its dissociation curve is a
rectangular hyperbola rather than a sigmoid curve
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 Shift to Right
 At any pO2 ,the O2 content that can be held by
blood decreases causing unloading of O2
 All the factors which shift ODC to right decrease the
affinity of Hb for O2 , therefore a higher pO2 is
required for hemoglobin to bind a given amount of
O2
 Therefore , CO2 enters the blood from tissues and
helps unloading of O2
 This phenomenon is called Bohr effect,ie:the
decrease in O2 affinity of Hb when pH of blood falls
 ie; Bohr’s effect is loading of CO2 to blood causes
unloading of O2, a phenomenon seen at tissue level
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Bohr effect
 The decrease in the O2 affinity of Hb when the pH of blood
falls due to increase in pCO2 is called Bohr effect.
 There is unloading of O2 from Hb.
 The ODC shifts to the right and P50 rises.
 This is because deoxyhemoglobin binds H+ more actively,
than oxyhemoglobin.
 Greater the CO2 tension in the tissue greater will be the O2
release.
 HbO2 + CO2 HbCO2 + O2
 HbO2 + H+ Hb H+ + O2
 All factors that shift ODC to the right influence Bohr effect

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 TRANSPORT OF CO2 IN BLOOD

Introduction to phsyiology of co2 transport

1. CO2 is the end-product of aerobic metabolism.

2. Produced almost entirely in the mitochondria
where the pCO2 is the highest
3. Elimination of CO2 - one of major requirement of
body.

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 CO2 DIFFUSION

• At each point in gas transport chain, CO 2 diffuses in

exactly the opposite direction to O2 diffusion.
• From tissue it moves to capillary blood
(arterial pCO2 = 40 mm Hg & tissues pCO2 =46 mmHg)
• From venous blood it moves to alveoli
(venous pCO2 = 46 mm Hg & alveoli pCO2 =40 mmHg)

• CO2 diffuses 20 times as rapidly as O2.

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 Different forms of CO2Transport in blood
Method Percentage
• As Bicarbonate Ion in 60-70% (70%)
Plasma
• As Carbamino compunds
Hemoglobin (carbamino Hb) 20 - 30 % (23%)
& Plasma proteins
(carbamino proteins)

• Dissolved in Plasma 7 - 10 % (7%)

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 1. CO2 BOUND AS HCO3

•  70% of CO2 transported from tissues to

lungs as bicarbonate.
• From tissues CO2 enters the RBC
• In the RBCs CO2 combines with H2O to form
Carbonic acid
• This reaction is very rapid due to the presence
of the enzyme carbonic anhydrase in the RBCs
CA
CO2 + H2 0 H2 CO3
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• Carbonic acid is highly unstable
• It dissociates into bicarbonate & hydrogen ions
H2 CO 3 H + + HCO -3
CA

• The bicarbonate ions diffuse through the cell

membrane into the plasma
• Here it combines with Na+ to form NaHCO3
• H+ is buffered by Hb
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Chloride shift or Hamburger phenomenon

• When HCO3- difuses from RBC to plasma, to

maintain electrical neutrality Cl- ions enter RBC
• This is called chloride shift
• The increase in Cl- ions inside the cell increases
the osmotic pressure inside the RBCs
• This draws water into the RBCs and it becomes
slightly larger.
• Thus PCV of venous blood is slightly larger than
that of arterial blood
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tissue plasma RBC

CO2 CO2 CO2 + H2O

H2CO3
CA C.A. = carbonic
anhydrase
HCO3- HCO3- + H+
Cl-
chloride Cl-

Shifts in H+ + Hb

Buffer
Action.
HHb

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Reverse Chloride shift (at lung level)

• This helps in the elimination of CO2 from the

blood into the alveoli ,when blood reaches the
alveoli
• Explanation :
• When O2 enters the RBC
• It displaces H+ from Hb & forms oxyhemoglobin
HHb + O2  HbO 2 + H+
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• The Na HCO3- in the plasma dissociates into Na
& HCO3- ions
• HCO3- moves into the RBC & Cl- moves out into
plasma, where it combines with Na+ to form
NaCl. This is called reverse Cl - shift
• The bicarbonate is converted back into CO2 as
it combines with H+
H+ + HCO3 H2O + CO2
• CO2 diffuses into the alveoli and is expelled
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 2. As Carbamino compounds

• 20-30% transported as carbamino compounds

combining with amino group of Hb & plasma
proteins as carbamino Hb & carbamino
protein

3. Dissolved form
• 10 % of CO2 is in dissolved form
• ie 2.5 ml of CO2 is dissolved in 100 ml of
blood
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26
 HALDANE EFFECT
• Importance : Haldane effect doubles the quantity of CO2
released from blood to the lungs and that is picked up
from the tissues into blood.
• Deoxygenated hemoglobin binds more CO2 than
oxyhemoglobin and forms carbamino hemoglobin and
Carbon dioxide dissociation curve shifts to left.
• Whenever hemoglobin is oxygenated ,it dispkaces CO2
from its combination and Carbon dioxide dissociation
curve shifts to right.
Causes
• Deoxyhemoglobin has more affinity for CO2 and so there is
increased pickup of CO2 from tissues
• Oxyhemoglobin has less affinity for CO2 and so CO2 is
released from blood to alveoli in the lungs
• Reduced Hb is a weaker acid & strong buffer
• Oxy Hb is a stronger acid & releases H+ at lung level 27