Introduction

Oxygen Transport
• The resting body requires 250ml of O2 per minute.
• O2 is transported by the blood either,
– Combined with haemoglobin (Hb) in the red blood
cells (>98%) or,
– Dissolved in the blood plasma (<2%).
• We have four to six billion haemoglobin containing
red blood cells.
• The haemoglobin allows nearly 70 times more O2
than dissolved in plasma.
 Haemoglobin
•Conjugated Globular protein

•Quaternary structure.

•Two alpha + 2 beta chains.

•Haem group at centre of each tertiary

structure (contains a ferrous ion Fe2+).
• Each haem group carries one molecule of O2.
• So
Hb + 4O2 HbO8
oxyhaemoglobin
• To be efficient haemoglobin must
– Readily pick up O2 at the gas exchange surface.
– Readily release O2 at those tissues requiring it.
• Haemoglobin molecules can transport up to four O2’s
– When oxygen binds to haemoglobin, it forms
OXYHAEMOGLOBIN;
– Haemoglobin that is not bound to oxygen is referred to as
DEOXYHAEMOGLOBIN.
• Co-operative binding: haemoglobin’s affinity for O2 increases
as its saturation increases.
• Oxygen binding occurs in response to the high PO2 in the
lungs
• When 4 O2’s are bound to haemoglobin, it is 100% saturated,
with fewer O2’s it is partially saturated.
• Haemoglobin saturation is the amount of oxygen bound by
each molecule of haemoglobin
• The graph on the following page shows an oxygen
dissociation curve, which reveals the amount of haemoglobin
saturation at different PO2 values.
• The Oxygen Dissociation Curve Reveals the amount of
haemoglobin saturation at different PO2 values.
The Oxygen Disassociation Curve
• Close to zero no O2
bound to
haemoglobin
• Low PO2
4polypetides chain
tightly bound, curve
rises slightly
• When 1 O2 binds to
haem groupmakes
it easier and curves
rises
• At high PO2
haemoglobin
saturated and curve
levels off
 The Bohr effect
 During respiration, CO2 is Red cell
produced. This diffuses into the
blood plasma and into the red
blood cells. plasma
 Inside the red blood cells are
many molecules of an enzyme
called carbonic anhydrase *. H2O
 It catalyses the reaction between
CO2 and H2O. CO2
* H2CO3
 The resulting carbonic acid then
dissociates into HCO3- + H+.
(Both reactions are
reversible). HCO3- + H+.

CO2 + H2O  H2CO3

HCO3- Cl-
carbon water carbonic
dioxide acid
 The Bohr effect (continued)
5. Haemoglobin very readily combines with
hydrogen ions forming haemoglobinic acid.
6. As a consequence haemoglobin releases
some of the oxygen it is carrying.
7. By removing hydrogen ions from the
solution, haemoglobin helps to maintain the
pH of the blood close to neutral. It is acting
as a buffer.
The Bohr effect (shift)

• CO2 reduces the

ability of Hb to
combine with O2.

• CO2 present at
respiring tissues –
so Hb releases O2.
 Why is the Bohr effect useful?
• High concentrations of carbon dioxide are
found in actively respiring tissues, which need
oxygen.
• Due to the Bohr effect, these high carbon
dioxide concentrations cause haemoglobin to
release its oxygen even more readily than it
would do otherwise.
 Factors affecting Disassociation
BLOOD TEMPERATURE
• increased blood temperature
• reduces haemoglobin affinity for O2
• hence more O2 is delivered to warmed-up tissue

BLOOD Ph
• lowering of blood pH (making blood more
acidic)
• caused by presence of H+ ions from lactic acid
or carbonic acid
• reduces affinity of Hb for O2
• and more O2 is delivered to acidic sites which
are working harder

CARBON DIOXIDE CONCENTRATION

• the higher CO2 concentration in tissue
• the less the affinity of Hb for O2
• so the harder the tissue is working, the more
O2 is released