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O2
dissolved
in
bloodstream
O2
transported
dissolved
in tissue
O2
Oxygen O2
98% travels in oxyhaemoglobin (in red
blood cells)
2% is dissolved in plasma
REMEMBER
Concentration of dissolved
oxygen is often referred as the
PARTIAL PRESSURE TENSION
O2
oxygen
HbO8
oxyhaemoglobin
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
Carbonic
anhydrase
H2CO3
Bohr Shift
Tissues
H2CO3
H+
Trapped in
cytoplasm
HCO 3
-
acidification
in the red
blood cell
With high
level of
activity
CO2 enters
the blood
Hb
affinity
with O2
Bohr Shift
Release
of O2
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
Bohr ing