Transport of O2 and CO2
The primary goal of respiration is to absorb
O2 from the environment to fuel the bodys
metabolism
O2 gas in
the inhaled
air
O2
dissolved
in
bloodstream
O2
transported
O2 used in the metabolism
of glucose and the synthesis
of ATP
dissolved
in tissue
O2
Movement of O2 in the body is a result of
its diffusion
The pressure of a gas is proportional to its density
of molecules and temperature
In a mixture of gas, we refer to the density of any
single molecular species as its partial pressure
If a solution of dissolved O2 is at equilibrium with
the adjoining air, the pO2 of the solution is the
same as that of the air
Diffusion occurs because:
The principle of diffusion: the gas will
diffuse from a point of high partial pressure
towards a point of low partial pressure
pO2(air)>pO2(interstitial fluid)>pO2(blood plasma)
Oxygen O2
98% travels in oxyhaemoglobin (in red
blood cells)
2% is dissolved in plasma
O2 is not very soluble thus needs a carrier !
REMEMBER
Concentration of dissolved
oxygen is often referred as the
PARTIAL PRESSURE TENSION
How is oxygen carried ?
HAEMOGLOBIN
Complex protein containing haem (iron)
1 molecule of haem combines with 4
molecules of oxygen to form oxyhaemoglobin
Hb +
Haemoglobin
O2
oxygen
HbO8
oxyhaemoglobin
This reaction is reversible.
Cooperativity
The haemoglobin molecule is a tetramer
composed of 4 protein subunits, each of which can
bind a single molecule to O2
These subunits exhibit cooperativity when they
bind to O2
i.e. the binding of O2 to any subunits increases the
likelihood that the other subunits will bind to O2
Release of O2
The release of O2 begins because metabolically
active tissue cells have consumed much of the O2
from the interstitial fluid around them
i.e pO2 (interstitial fluid)> pO2 (blood plasma)
O2 diffuses out of the capillary release of O2
bounded to haemoglobin
Haemoglobin combines with oxygen when it
is abundant and then releases it when the
concentration falls.
The cooperativity of O2 binding to
haemoglobin influences how much of the
blood O2 is delivered to any particular tissue.
This property is called an
OXYGEN DISSOCIATION CURVE
OXYGEN DISSOCIATION CURVE
Shows the amount of O2 that is bound
to haemoglobin (Y-axis) as a function
of the partial pressure of O2 in the
blood plasma (X-axis).
Because of the cooperativity, this
dissociation curve is S-shaped
OXYGEN DISSOCIATION CURVE
Bohr Effect or Bohr Shift
Niels Henrik David Bohr
Born: 7 Oct 1885 in Copenhagen, Denmark
Died: 18 Nov 1962 in Copenhagen, Denmark
Carbon Dioxide (CO2)
In red
blood
cells
70% travels as HCO3- ions
(hydrogencarbonate ions)
23% travels as carbamino
compounds
7% in plasma
CO2 = waste product of cellular metabolism
About 70% of the blood
CO2 reacts with H2O to form carbonic acid
CO2 + H2O
Carbonic
anhydrase
H2CO3
Carbonic acid rapidly dissociates into
H2CO3
H+ + HCO-3
ion H+ and bicarbonate ion
Bohr Shift
Tissues
H2CO3
H+
Trapped in
cytoplasm
HCO 3
-
Leaves the red
blood cell
acidification
in the red
blood cell
With high
level of
activity
CO2 enters
the blood
Hb
affinity
with O2
Bohr Shift
Release
of O2
Bohr Effect or Bohr Shift
The dissociation curve moves to the right at higher
concentration of carbon dioxide. This shows that
carbon dioxide lowers the affinity of Hb for
oxygen.
This means that when carbon dioxide
concentration is higher, Hb does not hold on to its
oxygen quite as well.
Hb tends to give up O2 in area of high CO2 such
as the respiring tissues that need it most.
Effect of pH (temperature = 38oC)
Saturation of haemoglobin (%)
High blood pH
(Low CO2)
pH 7.6
Normal acidity
pH 7.4
pH 7.2 - low
blood pH (High
CO2)
8
PO2/KPa
12
Foetal haemoglobin
Foetal haemoglobin has a higher
affinity for oxygen than adult
haemoglobin.
This means that the foetus can
receive oxygen from the mother
across the placenta.
Myoglobin
Myoglobin is a pigment found in
muscles, particularly in legs and heart
muscles of mammals
Like Hb, myoglobin can reversibly
bind O2 (only one), it acts like a
temporary store of oxygen
Hope this presentation
wasnt
Bohr ing
