Gas Transport in blood and

O2- Hb dissociation curve

Dr Masolwa Ngwanasayi
Group 1
Facilitator: Dr. B.L. Mtinangi
 Layout
Introduction
Oxygen Transport
Uptake of O2 during exercise
Hb molecule
O2-Hb dissociation curve
Factors affecting O2-Hb dissociation curve
Myoglobin
Carbon dioxide transport
Forms of CO2 transport in blood
CO2 release in the lings
 Introduction
Gases move from one point to the another by
diffusion
Usually down a concentration gradient, from a
point with high partial pressure to a point with
low partial pressure.
The partial pressure gradients for O2 and CO2
are the key to gas movement
O2 "flows downhill" from the air through the
alveoli and blood into the tissues
whereas CO2 "flows downhill" from the tissues to
the alveoli.
 Intro
However, 97-99% of the O2 which dissolves in
blood combines with hemoglobin.
The presence of hemoglobin increases the O 2-
carrying capacity of the blood 70-fold.
About 94.5% of the CO2 which dissolves in blood
enters into a series of reversible chemical
reactions that convert it into other compounds.
These reactions increase the blood CO2 content
17-fold.
Pressure Gradients Gas
Transport
Push gases in and out mm
Hg
Pressure gradients drive O2 toward cells; drives CO2 towards lungs.

pO2 and pCO2 at various stages in gas transport

Cells Interstitial Venous Arterial Alveolar Expired Air

23 30 40 95 100 115 158 O

O22

CO
CO22 60 50 45 40 40 32 0.3

Note: pO2 is the partial pressure oxygen (or oxygen tension).

pCO2 is the partial pressure of carbon dioxide.
 Oxygen Transport
Oxygen delivery to tissues depends on
Amount of O2 entering the lungs
Adequacy of pulmonary gas exchange
Blood flow to tissues
Capacity of blood to carry oxygen
 Blood flow depends on
The degree of tissue vascular constriction
Cardiac output

Amount of O2 in blood depends on

Amount of dissolved oxygen
Amount of Hb in blood
Hb affinity for oxygen
 Uptake of O2 by the pulm blood
during exercise
Diffusion capacity for O2 3x due to increased
capillary surface area; and ideal ventilation
perfusion ratio in the upper parts of the lungs
Since under normal conditions blood becomes
almost saturated by the time it passes through
1/3 of the pulmonary capillary.
Therefore, even with shortened time of
exposure, the blood can still become fully
saturated
 Hemoglobin molecule
Is a protein made up of four subunits,
each of which contains a heme moiety
attached to a polypeptide chain.
In normal adults, most of the hemoglobin
molecules contain two and two chains
Heme is a complex made up of a
porphyrin and one atom of ferrous iron.
Each of the four iron atoms can bind
reversibly one O2 molecule.
 Hb.
The quaternary structure of hemoglobin
determines its affinity for O2.
In deoxyhemoglobin, the globin units are tightly
bound in a tense (T) configuration which reduces
the affinity of the molecule for O2.
When O2 is first bound, the bonds holding the
globin units are released, producing a relaxed (R)
configuration which exposes more O2 binding
sites.
The net result is a 500-fold increase in O2 affinity.
In the tissues, these reactions are reversed,
releasing O2.
 Hb
When fully saturated, each gram of normal
hemoglobin contains 1.34 mL of O2.
The hemoglobin concentration in normal blood is
about 15 g/dL.
Therefore, 1 dL of blood contains 20.1 mL (1.34
mL 15) of O2 bound to hemoglobin when the
hemoglobin is 100% saturated.
200 ml O2 carried per liter x 5 liters 1000
ml O2 carried/min
However, tissues use only 250 ml O2 per minute
only 25% of O2 molecules are used.
O2-Hb dissociation curve
 P50
Is the PO2 at which Hb is 50% saturated
with oxygen.
The higher the P50 the lower the affinity of
Hb for oxygen.
When the curve is shifted to the Right,
affinity of Hb to O2 is reduced, and the P50
increases.
Therefore, a higher PO2 is required for
hemoglobin to bind a given amount of O2
4 factors affect affinity of Hb to O2-
The O2-Hb dissociation curve
A fall of pH shifts the curve to the Right.
This is known as Bohr effect
Increased CO2 concentration
A rise in temperature shifts the curve to
the Right, and vice versa.
An increase in the concentration of 2,3-
DPG shifts the reaction to the right, and
vice versa.
 Effect of CO2 and H +

As the blood passes through the tissues, carbon

dioxide diffuses from the tissue cells into the
blood. This increases the blood PCO2, which in
turn raises the blood carbonic acid (H2CO3) and
the hydrogen ion (H+) concentration.
These effects shift the oxygen-hemoglobin
dissociation curve to the right and downward
forcing oxygen away from the hemoglobin and
therefore delivering increased amounts of
oxygen to the tissues. This phenomena is called
the Bohr effect.
Exactly the opposite effects occur in the lungs.
Integrated CO22/O22 Transport Gas Transport
At the Cells Overview
Plasma
RBC CO2
40 mmHg
R-NH2 CO 1 dissolved CO Cel
32% 2 2

R-NHCOO CAaseH 2 O ~5%m

2plasma COl 2
+ H+ H CO 45 mm Hg
2 3 RNHCO2-
Bohr Effect
23 mmHg
+H
+
+ HCO3 3
HCO3 O2
HbO2 HHb + Cl- 60%
venous 75% sat.
O2 Cl
(H2O)
O2
Integrated CO22/O22 Transport Gas Transport
At the Alveoli Overview

RBC Plasma
R-NH2 CO CO2 CO Alveo Alveol
11% 2 1 45 mmHg
R-NHCOO- H O dissolved CO2 CO2
CA as 2
+ H+ H COe 5% 40 mm Hg
2 3 2
Alkaline Bohr plasma
RNHCO2
- 100 mm
+ H+
+ HCO 3 3
HCO3- O2
HbO2 HHb + Cl- 70%
90% vol.
O
arterial 96% sat. 2
Cl-
(H2O)
O2
0.3Vol%
 2,3-diphosphoglycerate
Is plentiful in RBCs, with t1/2 of 6hrs
Is a highly charged ion that binds to the beta
chains of deoxyhemoglobin, to release oxygen
Its conc is Alkalosis, Thyroid hormones,
Growth hormones, Androgens, exercise, ascent
to high altitudes, and in diseases characterized
by chronic hypoxia e.g. anemia.
Its conc is by acidosis
Preserved in blood bank by citrate-phosphate-
dextrose solution.
 Fetal Hb
HbF has greater affinity for O2 than HbA,
to facilitate movement of O2 from the
mother to the fetus
This is due to poor binding of the 2,3-
DPG by the polypeptide chains that
replace - chains in fetal Hb.
 Myoglobin
An iron containing pigment found in skeletal
muscles, especially those specialized for
sustained contractions.
Resembles Hb but bind to 1 rather than 4 moles
of O2 per mole.
Its dissociation curve is a rectangular hyperbola,
to the Left of the Hb curve.
It takes up O2 from Hb in the blood
Releases O2 only at very low PO2, e.g. in
exercising muscles
Hb & Myoglobin dissociation curve
 CO Poisoning
CO combines with Hb at the same point on the
Hb molecule as does O2, thereby displacing O2,
and its O2 carrying capacity
CO has 250x more binding affinity to Hb as
compared to O2. It combines with Hb at very low
partial pressures (0-0.4mmHg).
Even though O2 content in blood is greatly in
CO poisoning, but the PO2 may be normal.
This makes exposure to CO especially
dangerous, because blood is bright red, and no
signs of hypoxemia e.g. cyanosis.
 CO poisoning
As a consequence, the feedback mechanism that
usually stimulate RR in response to lack of O2 is
absent.
Pt may become disorientated, unconscious, and
even die without any feedback respiratory
response.
Treatment is usually by giving pure O2, because
O2 at high alveolar pressure can displace CO from
its combination with Hb.
Simultaneous administration of 5% CO2 stimulate
the Respiratory centre to alveolar ventilation,
and reduce alveolar CO2
 Carbon dioxide Transport
The solubility of CO2 in blood is 20x that of O2.
So there is considerable more CO2 than O2 in
simple solution at equal partial pressures.
Under normal resting conditions, 4mls of CO2 is
transported from the tissues to the lungs in each
100mls of blood. Equivalent to 200mls of CO2 in
each 5L of blood.
However, CO2 in blood has a lot to do with acid-
base balance of the body fluids.
Chemical forms of CO2 transport in
blood
CO2 is transported in 3 different forms
1.Small amount is transported in dissolved form in
plasma, as CO2 molecule.
2.7mls/dl at 45mmHg in venous blood, and
2.4mls/dl at 40mmHg in arterial blood.
Therefore, only about 0.3mls of CO2 is transported in
dissolved state for each 100ml of blood.
2.As bicarbonate ion. Account for 70% of CO2 transport
3.In combination with Hb and plasma proteins. Account
for about 11% of CO2 transport
 As bicarbonate ion
Dissolved CO2 in RBC quickly react with water-
in the presence of Carbonic Anhydrase, to form
Carbonic acid.
In another fraction of a second, the carbonic acid
formed in the red cells (H2CO3) dissociates into
hydrogen and bicarbonate ions (H+ and HCO3)
Most of the H+ combine with Hb in RBC, bse Hb
is a powerful acid-base buffer
Many of the HCO3- diffuses into plasma, while in
exchange Cl- diffuses into RBC.
Thus, Cl- content is higher in venous RBCs than
in arterial RBCs. A phenomenon called Chloride
shift.
 In combination with Hb & plasma
proteins
Some of the CO2 in RBC reacts with amino
groups of Hb, forming carbaminohemoglobin
(CO2Hgb)
This combination of carbon dioxide and
hemoglobin is a reversible reaction that occurs
with a loose bond,
carbon dioxide is easily released into the alveoli,
where the PCO2 is lower than in the pulmonary
capillaries
CO2 also reacts similarly with plasma proteins.
However, this is not significant.
CO2 uptake
 Release of CO2 in the lungs
Binding of oxygen with hemoglobin tends to
displace carbon dioxide from the blood. This
effect, called the Haldane effect,
This effect is quantitatively far more important in
promoting carbon dioxide transport than is the
Bohr effect in promoting oxygen transport.
It results from the simple fact that the
combination of oxygen with hemoglobin in the
lungs causes the hemoglobin to become a
stronger acid.
This displaces carbon dioxide from the blood and
into the alveoli in two ways
 CO2 Release..
1. The more highly acidic hemoglobin has less tendency to
combine with carbon dioxide to form
carbaminohemoglobin, thus displacing much of the
carbon dioxide that is present in the carbamino form
from the blood.

2. The increased acidity of the hemoglobin also causes it

to release an excess of hydrogen ions, and these bind
with bicarbonate ions to form carbonic acid; this then
dissociates into water and carbon dioxide, and the
carbon dioxide is released from the blood into the alveoli
and, finally, into the air.
CO2 Release.
 References
William F. Ganong. Review of Medical
Physiology. 21st ed, 2003
Guyton, A.C. Textbook of Medical
Physiology. 11th ed, 2006
Various internet sources