Trans. of Oxygen

Transport Of Oxygen
Dr.Parijat Biswas
MBBS,MD (Physiology)
O2 Transport
• O2 transport depends on both di usion and the flow

of blood
• Gases moves from one point to another by

di usion
• This movement occurs due to partial pressure

di erence from first point to the next
A)Transport of O2 From Alveolar Air into
Pulmonary Capillary
• From atmosphere to lungs :

By pulmonary ventilation
• Di usion of O2 from the alveoli to the
pulmonary capillary-
* Po2 in the alveolus=104 mm of Hg

* Po2 in pulmonary capillary at arterial
end=40 mm of Hg
* Pressure di erence=(104-40) mm of
Hg=64mm of Hg
Fig: Uptake of O2 by the pulmonary capillary blood (Hall 2011)
B)Transport of O2 in the blood
• PO2 in the venous end of the pulmonary capillary=104
mm of Hg,
• In the systemic artery is reduces to 95 mm of Hg
This alveolar-arterial oxygen di erence is due to:
Physiologic Shunt: A small amount of blood from the

myocardium & that from the bronchial tree drains back
into the systemic circulation & is not oxygenated in the
lungs.
O2 is transported in the blood in
two forms:
1.In Dissolved state – about 3%
• The significance of the dissolved O2 is that “It is

responsible for the PO2 in the blood which is very
important for both binding with Hb and delivery to
tissue”.
2.In combination with O2-Hb-about 97%

In combination with Hemoglobin:
• Binding of oxygen with hemoglobin is a loose and
reversible bond ,called oxygenation not oxidation.
• Here iron stays in ferrous(Fe++) form not

ferric(Fe+++) form.
C)Delivery Of O2 From blood to the
tissue Space
• From blood to
interstitial space: The
PO2 in the arterial
blood is 95 mm of Hg
& in the interstitial
space is about 40 mm
of Hg. Therefore O2
enters into the
interstitial space at a
pressure gradient of
55 mm of Hg.
Fig:Di usion of O2 from a pulmonary

capillary to the cell
(Hall2011)
D)From the interstitial space to cell
• The PO2 interstitial
space is about 40
mm of Hg & inside
the cell is about 23
mm of Hg,partial
pressure di erence
is 17 mm of Hg.
Fig:Di usion of O2 from a pulmonary

capillary to the cell
(Hall2011)
Oxyhemoglobin Dissociation Curve
• Oxygen hemoglobin
dissociation curve
relates percentage
saturation of the
oxygen carrying
power of hemoglobin
to the PO2.
• The curve has
following
characteristics:
Fig:Oxyhemoglobin dissociation curve
• The curve is sigmoid(Hall2011)
shaped due to T-R
Fig :Oxyhemoglobin Dissociation Curve (Barrette et
al .2012)
Loading(Association)zone:
• Loading zone of the
oxyhemoglobin
dissociation curve is the
plateau that occurs
above Po2 of
approximately 60mmHg.
This zone provides a
margin of safety,
because the alveolar Po2
can be reduced
substantially,yet the
hemoglobin saturation
remains quiet normal. Fig:Hemoglobin saturation with oxygen
tension of the blood
(www.medical-dictionary.thefreedictionary.
com)
Unloading(Dissociation)zone
• The unloading zone of
the curve in the steep
portion of the curve
that occurs at Po2
below 60mmHg.This
zone allows
hemoglobin to release
large amount of
oxygen in response to
relatively small
changes in Po2.
Fig:Hemoglobin saturation with oxygen
tension of the blood (www.
medicaldictionary.thefreedictionary.com)
P50
• It is the Po2 at which the Hb is 50% saturated
with O2.It is the index of shifting of the curve.
P50 is 28- 30 mmHg
• Signifance: P50 = a nity of Hb for O2 & 

release of O2 to the tissue
Factors for P50
Factors that increases Factors that
P50 decreasesP50
• Acidosis • Alkalosis
• Increases Co2 • Decreases Co2
concentration concentration
• Increases blood • Decreases blood
temperature temperature
• Increases 2,3 BPG • Decreases 2,3 BPG
Shifting of Oxyhemoglobin
Dissociation curve
• The Oxyhemoglobin Dissociation curve is
influenced by:
1. Partial pressure of CO2 (Pco2)
2. H+ concentration (i.e. pH)
3. Temperature
4. 2,3 biphosphoglycerate (2,3BPG)
• The shifting of the curve to the right indicates the
reduction of hemoglobin a nity for
oxygen (i.e. O2 is released to the tissue) &
shifting of the curve to the left indicates the
increase in hemoglobin a nity for oxygen (i.e.
O2 is bound to hemoglobin as occur in the
lungs)
Pco2
The concentration of CO2 in the red cells,
influences shifting of the curve. The
curve shifts to the left when Pco2 decreases &
vice versa.
pH
• The curve will move
to the right in the
presence of acidosis
(metabolic or
respiratory). A
decrease in
Hydrogen ion
concentration shifts
the curve to the left
Fig :E ect of pH on the Oxyhemoglobin

Dissociation Curve (Hall2011)
Temperature
•Increase temperature will
shift the curve to the right.
•Decrease temperature
will shift the curve to the
left.
Fig :E ect of temperature on the

Oxyhemoglobin Dissociation Curve
(Barrette et
al .2012)
2,3 Biphosphoglycerate
• 2,3 biphosphoglycerate(2,3 BPG) is formed in red
cell from 3-phosphoglyceraldehyde,which is a
product of glycolysis via Embden-Mayerhof
pathway.
• 2,3-BPG is a highly charged anion binds to the

beta chains of deoxyhemoglobin.
• HbO2 + 2,3 biphosphoglycerateHb-2,3-BPG +O2

Therefore an increase in 2,3 biphosphoglycerate
shifts the oxyhemoglobin curve to the right & vice
versa.
• Anaemia, hypoxia, thyroid hormone,
growth hormone, exercise,high altitude
and increase Ph ,increase the
concentration of 2,3-BPG in the red
blood cell and increase P50.
Shifting the curve to the right
• Increase Pco2 • (
• Acidosis (decrease
pH)
• Increase
temperature
• Increase 2,3 BPG
• Sickle hemoglobin
• Anaemia
(Hall 2011)
Shifting the curve to the left
Causes:
• Low H+
• Low temperature
• Low 2,3 DPG
• Low PCO2
• Variants of normal Hb (Fetal-Hb )
Myoglobin
• Iron containing pigment in skeletal muscle
similar to Hb. Its dissociation curve is
rectangular hyperbola rather than a sigmoid
curve and to the left. It takes up oxygen from
Hb.
• It releases oxygen only at low Po2 values.e.g.in
exercising muscle the Po2 is close to zero.
• During sustained contraction, when the blood
flow is cut o , myoglobin may provide O2.
Bohr E ect
The decrease in O2 a nity of Hb, when the PH
of blood falls & Pco2 increases is called Bohr
E ect & is closely related to the fact that the
deoxygenated Hb binds H+ more actively.
Mechanism of Bohr E ect
The Bohr e ect reflects the fact that the
deoxy form of hemoglobin has a greater
a nity for protons (H+) than does
oxyhemoglobin. The Bohr e ect can be
represented schematically as:
CO2+H2O  H2CO3  HCO3 - +H+

HbO2 + H+  HbH + O2
(Oxyhemoglobin) (Proton)
(Deoxyhemoglobin)
Importance of Bore e ect
• 1) In lungs: In lung it increases the a nity
of Hb for oxygen, thus increases the
oxygenation of pulmonary blood.
• 2) In tissue: In tissue it decreases the
a nity of Hb for oxygen, thus increases
oxygen delivery to the tissue.
Continued…
• When blood passes through the tissues,carbon
dioxide di uses from the tissue cells into the blood.
This increase the blood Pco2,which in turn raises the
blood carbonic acid and hydrogen ion
concentration.This e ect shift the oxyhemoglobin
curve to the right.
• Opposite e ect in the lungs,CO2 di uses from the
blood into the alveoli.this reduces the blood Pco2
and decreases the hydrogen ion concentration,
shifting the oxyhemoglobin curve to the left.
Double Bohr e ect
During pregnancy , In
placenta Oxygen Hb
dissociation curves for
maternal HbA and
fetal HbF move in
opposite direction. This
is known as double
Bohr e ect.
Tissue O2 bu er function of
hemoglobin
• Hemoglobin maintains nearly constant Po2 in the
tissues, when the atmospheric Po2 changes from
60mmHg to 500mmHg.
• During exercise about 75% O2 release from Hb to

the tissues with little decrease in the tissue Po2.
Thank
you

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Transport Of Oxygen

• O2 transport depends on both di usion and the ﬂow

• Gases moves from one point to another by

• This movement occurs due to partial pressure

• From atmosphere to lungs :

* Po2 in the alveolus=104 mm of Hg

This alveolar-arterial oxygen di erence is due to:

Physiologic Shunt: A small amount of blood from the

• The signiﬁcance of the dissolved O2 is that “It is

2.In combination with O2-Hb-about 97%

• Here iron stays in ferrous(Fe++) form not

Fig:Di usion of O2 from a pulmonary

Fig:Di usion of O2 from a pulmonary

• Signifance: P50 = a nity of Hb for O2 & 

Fig :E ect of pH on the Oxyhemoglobin

Fig :E ect of temperature on the

• 2,3-BPG is a highly charged anion binds to the

• HbO2 + 2,3 biphosphoglycerateHb-2,3-BPG +O2

CO2+H2O  H2CO3  HCO3 - +H+

• During exercise about 75% O2 release from Hb to

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