TRANSPORT OF
OXYGEN
Overview
C
Fi
(Cold) Air 70x =
160mmiy
-
100 -
O
=
Por + Pn+ ProstPazo
PHzo
= 4
Emmity POz (PB-Phzo) Fio ~ 149 7
·
.
=
at 37% I
o mmitg
fraction
Fio
-
in
Inspiration Por Bio-Oconeempt
=
16
Expi
.
FeOr- ↓ t
producti
co p l
a
- R Q= - a -
-
.
E
Patr =
[Pz02-
PaOz =
((PB-Pgo) Fio -
~ 104 enmity
Alveolar gas equation
Hyperbaric oxygen
Hyperbaric oxygen: 100 percent oxygen at two to
three times the atmospheric pressure at sea level
() D
Shint
PO
= 100
Simple diff
-
th
-
por = 10
-
A T
95-98mmltg
002 40
= Asterial
95-98
Physiological Shunt
mmltg
%
2
0
oommig
O2 Cascade
• Alveolar air pO2: 100-104 mm Hg
• Arterial blood pO2: 95 mm Hg
• Venous blood pO2: 40 mm Hg
• Tissue interstitial fluid pO2: 40 mm
Hg
Steps in transport of Oxygen
• Transport of oxygen from the lungs to the tissues can be
described as under:
O
1. Uptake of oxygen in the lungs by pulmonary blood
O
2. Transport of oxygen in arterial blood
O
3. Release of oxygen from blood to the tissues.
Uptake of oxygen in the lungs
• pO2 of pulmonary arterial blood is about 40 mm Hg and that of
alveolar air is 104 mm Hg.
• Oxygen readily diffuses from the alveoli into the blood.
Transport of oxygen in arterial blood
Transport occurs via two processes:
• Hemoglobin bound O2 (99%)
• Dissolve O2 (1%)
Dissolve O2
Law Sole Co-effic
Depends Henry's
-
on >
-
DOz =
(Solubity <PO2) 03
-vous
Arterial
(P02 40)
=
(0 003 x 40)
-
(0 003x98) Doz
.
.
=
D02
=
= 0 .
12 m/dl
= 0 .
29 m/dl
Hb-Bound O2
Depends on saturation of Hb
↓
.
(SO2/SpO2
saturation depends
Partial pressure (PO2)
ABG()
When POz =
120 mmig
-s 502 = 100% PURE
Ign LHb
of
= 1 .
39m02
Hb 1 34 m 02
Igm
.
=
-
(in real life)
when PO2 = 98 minity
S0297%
15
gmy .
IgmHb
=
(34x
29m) 02
Htb-bound (1 29x15) ~ 1
.
Total =
.
-
~ 19 3.
mr/dl -
PO2 40 S02 x
=
when = 75%
Igm
Hb =
(1 .
34
-1 01 ml 02
.
G
15 ga % Total = 15x1 :
01 = 15 I .
m
Arterial blood
- Hb-bound)
Total Of
= (D02 +
zome/de
(0 .
29 + 19 .
3) I
(CaO2)
=
Venous blood
-
(15 .
1 + 0 .
(2)
Toful 02
=
T 15 2 .
mr/Al
⑧ 80 %
PaO2
Y
Or
C
Pa02 Altitude
PaO2 Anemia
S
High
Age
?
-
=
Poor -
-
PO2 = N = N PB ↓↓
N 502 = N Post
SO2 =
J
L i
Pulse Oximetry: oxygen saturation (SO2)
Arterial blood gas (ABG) test
ABG test measures the blood gas tension values of the arterial partial
pressure of O2, CO2, blood's pH and electrolytes
Dissolve O2
• The dissolved oxygen obeys the Henry’s law, i.e. amount dissolved is
proportional to the pO2.
• Dissolve oxygen per dL (100 mL) of blood = (Solubility oxygen ✖ pO2)=
(0.003 ✖95) = 0.28 mL
• Thus, there is no limit to the amount of O2 that can be carried in dissolved
form, provided the pO2 is sufficiently high.
Hb-Bound oxygen
• Hb-bound oxygen depends on saturation of Hb (SO2/SpO2)
• SpO2 depends on PO2
• When, PO2 = 120 mmHg, Hb is 100% saturated (fully
saturated).
• 1g of fully saturated pure Hb can carry 1.39 mL of oxygen
Hb-Bound oxygen
• O2 capacity of pure 1gm Hb is ∼1.39 mL O2 when the hemoglobin is 100%
saturated AND assuming that no impure form of Hb (metHb) is present.
• In real life, the O2 capacity may be closer to 1.34 mL O2/g Hb because
small quantities of inactive hemoglobin derivatives (e.g., metHb/Hb-CO)
• When Hb is 97% saturated, 1gm Hb will carry
% Saturation of Hb
= ________________
O2 capacity of Hb ✖ = 1.34 ✖ 97/100 = 1.29 ml
100
Release of oxygen from blood to the tissues
• Arterial blood contains about 20 mL and venous blood about 15
mL of O2 per 100 mL.
• Thus, ~5 mL of O2 is transported per 100mL of blood from the
lungs to the tissue cells.
Tissue release of oxygen
• At rest the tissues remove about 4.6 mL of O2 from each
deciliter of blood passing through them
• 0.17 mL dissolve O2 and the remainder O2 liberated from Hb.
• In this way, 250 mL of O2 per minute is transported from the
blood (total blood volume 5000 mL)to the tissues at rest.
Release of oxygen from blood to the tissues
20 15
Ca02 =
CrO2 =
OSu
release
Tissul
Summary
100
Arterial
-
venous
-
A
POz =
95-98mmity
POL= 40 So2 = 97%
So2 = 78% Co02 = zovlIde
Crop = 15m/dl
Tissue
2
Summary of oxygen transport
From the lungs, the amount of O2 loaded by 100 mL of blood:
• Whole blood : 19.8 mL
• Haemoglobin solution : 19.5 mL
• Plasma solution : 0.29 mL only
In the venous blood at pO2 of 40 mm Hg, the amount of oxygen in100
mL of blood is:
• Whole blood : 15.2 mL,
• Haemoglobin solution : 15.1 mL and
• Plasma : 0.12 mL
Oxygen-hemoglobin dissociation curve
SO2
POz So2
S Fi
- a
100%
-
0 >
-
%
0
- 50%
26
40 - 75% 50% -
98 - 97%
120 - 100%
to
H 23-26
mmity iso
-
OHDC
Shift OHDC
Right
-
Fin S
① P50 increases
in
② Decrease
of affinity
↑ release of
at tissue
(unloading of↑
I Hb)
P50
Right Shift
Causes of
-
↑
Temp .
Ces . Exercise)
↑ PCO2 Right
Direct eff
-
-
↑ H +
(Acidosis) -
shit .
(Arute)
↑ 2 , 3 DPG
- Indirect - Left-shift
↑ Hypoxiae
Chronic)
-
>
-
vid
EGH Phy
,
The Luebering-Rapoport pathway: 2,3-BPG
Acidosis
Glyceraldehyde 3-phosphate
G
Bisphosphoglycerate
mutase
1,3-Bisphosphoglycerates
phosphoglycerate
Kinase 2,3-Bisphosphoglycerate
3-Phosphoglycerate
2-3 Bisphosphoglycerate
phosphatase
shift nhDPG
&
D
.
↓ Tempo
-
↓ PCO2
t
↓ If +
of blood
storage
E
Foetal blood
co-poisoning ·
2
-
Met-Hb .
Elow
·
.
stage
affinite
OHDC in different conditions
Rectangular hyperbola
O2-Hb dissociation curve of fetal haemoglobin
• Foetal Hb (HbF) contains two gamma (γ) chains rather than beta (β)
chains of HbA
• HbF have very little affinity for 2,3-DPG as compared to the adult Hb.
• The O2–Hb dissociation curve of HbF is shifted to left because oxygen
affinity of Hb increases
Stored blood: decrease 2,3 BPD/2,3 DPG
• Storage of blood generally done in acid citrated buffer solution.
• Acidic solution inhibits glycolysis in RBC as well as Bisphosphoglycerate
mutase enzyme
• So, during storage, RBC rapidly lose 2,3-DPG leading to an increase in
-
the affinity for O2 and a temporary impairment of O2 transport.
Effect of carbon monoxide (CO)
• Carbon monoxide (CO) about 200 times the affinity (of oxygen) for
haemoglobin.
• CO combines with Hb at the same site on its molecule as O2 and forms the
carboxyhaemoglobin.
• In the presence of CO, the affinity of Hgb for O2 is enhanced.
--
• Defective release of other O2 molecule
--
• CO decrease the O2 content of blood and thus hypoxia.
-E
OHDC for myoglobin
• Myoglobin is present in higher quantities in the muscles.
• Resembles hemoglobin but binds 1 rather than 4 mol of O2 per mole
protein.
• Lack of cooperative binding
• Dissociation curve is rectangular hyperbola rather than sigmoid in shape
• Myoglobin does not show the Bohr’s effect.
High Altitude adaptation
• Decrease of the PO2 of RBCs stimulates glycolysis, leading to increased levels of
2,3-DPG.
• Hypoxia stimulates RBC glycolysis by promoting release of all glycolytic enzymes
from Band 3 on RBC membrane
• Chronic hypoxia, anemia, and acclimation to high altitude are all associated with
an increase in 2,3-DPG levels
n
• Oxygen affinity of hemoglobin decreases
• More oxygen delivery to tissue
CO2 transport
Overview
↓
Ploz = 40
PC02 = 46a
content = 48ml/dl
Contentm/A
2 i I sm
relase Tissue
Methods of Co2 transport
Plasma RBC
Dissolve CO2 O
5% O
5% Dissolve CO2
CO2-NIR
% CO2 NID 33-
Carbamino Carbamino %
Compound O
1% O
21%
Compound
CA + 5000 timefaster
Bicarbonate
formation O5% O
63%
Bicarbonate
formation
CA
CO2+ 120 -
12
+
H
At tissue: Bohr effect
02 relesse
Tissue
CO2
↓ & O2
Hoz-
M
+
+
0%
Hb02- Hitb
+o
#mosto
2
ItbOr 120 + co2 -12lobH5
Hoz
Chloride Shift or,
Hamburger
Eff -
Bohr effect
• When pH is lowered (or PCO2 raised), the oxygen affinity of the blood
decreased (increased P50) leading to release of O2 to tissue.
• Bohr effect refers to right shift in oxygen dissociation curve caused by
changes in the concentration of CO2 or pH.
• The separate effects of H+ and CO2 are qualitatively similar, but the effect
of H+ (pH Bohr effect) is much stronger than the CO2 effect in lowering
oxygen affinity.
At lungs: Haldane effect
wor retake
or
de
vo
Hitb
-Hb -
202
163
↑
O
O
- H20
Haldane effect
• Oxygenation of blood in the lungs displaces CO2 from hemoglobin,
increasing the removal of CO2.
• The Haldane effect describes the shift in the CO2 dissociation curve
caused by oxygenation of Hb.
• Haldane effect approximately doubles the amount of CO2 released from
the Hb in the lungs and doubles the pickup of CO2 in the tissues.
At Tissue
Bohr Effect
Chloride shift or, Hamburger Shift
At Alveoli
Haldane Effect
At tissue level
PO2= 40 mmHg
A Haldane effect
52
CO2 in blood
C
50 At Lung level
PO2= 100 mmHg
48
B
40 46 PCO2
Bohr Effect
• The effect of CO2 and H+ on hemoglobin’s affinity for O2
is known as the Bohr effect.
• There is a decrease in O2 affinity of Hb with a decrease
in pH
• Rightward shift of the oxygen equilibrium curve resulting
from a rise in blood CO2 and H+ on is Bohr effect.
Haldane Effect
• When O2 binds with hemoglobin, CO2 is released to increase
CO2 transport.
• The binding of O2 with Hb molecule in the pulmonary capillary
tends to displace CO2 from the Hb (blood).
• Haldane effect is quantitatively more important in promoting
CO2 transport than is the Bohr effect in promoting O2 transport.
The Haldane effect results from:
• Combination of O2 with hemoglobin in the lungs causes the hemoglobin to become a
stronger acid. This displaces CO2 from the blood and into the alveoli in two ways.
• More highly acidic hemoglobin has less tendency to combine with CO2 to form
carbaminohemoglobin, thus displacing much of the CO2 that is present in the
carbamino form from the blood.
• Increased acidity of the hemoglobin also causes it to release an excess of hydrogen
ions, and these ions bind with bicarbonate ions to form carbonic acid, which then
dissociates into water and CO2, and the CO2 is released from the blood into the
alveoli and, finally, into the air.
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