How Are Oxygen and Carbon Dioxide Transported in Blood?

CONCEPT : Blood is a connective tissue that consists of cells in a

watery extracellular matrix. Besides carrying oxygen and

carbon dioxide between cells and the lungs, blood transports
nutrients from the digestive tract to other tissues in the body,
moves waste products to the kidney and liver for processing,
conveys hormones from glands to target tissues, delivers
immune system cells to sites of infection, and distributes heat
throughout the body.
CONCEPT : Oxygen Molecule is Non Polar, so solubility in blood plasma
less. Then how is Oxygen Transported in Blood?
Hemoglobin (a protein molecule) combines reversibly with up to 4 O2
molecules and increases the capacity of blood to transport O2 by about 60fold, making high levels of metabolism in higher animals possible.

So, Transport of Oxygen

97 % RBCs
3 % dissolved state in the plasma.

Hemoglobin picks up O2 where PO2 is high and release it where PO2 is lower.

CONCEPT : Oxygen

Delivery by Hemoglobin Is Extremely

Efficient due to cooperative binding and the Bohr shift.

O2 saturation (%) of hemoglobin

Cooperative binding is important because it makes hemoglobin

exquisitely sensitive to changes in the of values of PO2 in tissues.
% O2 changes
slowly

100
80
60

In this part of the graph, a

small change in PO leads to
2
a large change in how much
O2 unloads from hemoglobin

40
% O2
changes
slowly

20
0

20

40

60

80

PO2 (mm Hg) in blood within tissue

FIGURE 45.14 The OxygenHemoglobin Equilibrium Curve Is
Sigmoidal. A sigmoidal curve has three distinct regions.

100

The most remarkable feature of the oxygenhemoglobin equilibrium curve is that it is sigmoidal, or S-shaped. The pattern occurs because the binding of each successive oxygen molecule to
a subunit of the hemoglobin molecule causes a conformational
change in the protein that makes the remaining subunits much
more likely to bind oxygen.

Conversely, the loss of a bound oxygen molecule changes

hemoglobins conformation in a way that makes the loss of
additional oxygen molecules more likely.

100
80

Resting

40

Exercising

er
op
Co

20
0

ind
i

ng

60

at
ive
b

O2 saturation (%) of hemoglobin

(a) With cooperative binding, large amounts of O2

are delivered to resting and exercising tissues.

20

30

40

60

80

100

PO2 (mm Hg) in blood within tissue

O2 saturation (%) of hemoglobin

(b) Without cooperative binding, smaller amounts of O2

would be delivered to resting and exercising tissues.
100
Resting

80

Exercising
e
iv
at
r
pe
oo
c
on
N

60
40
20
0

20

30

ng

di

n
bi

40

60

80

PO2 (mm Hg) in blood within tissue

100

Sub Concept : Hemoglobinlike other proteinsis sensitive

to changes in pH and temperature.

O2 saturation (%) of hemoglobin

As noted above, the temperature and partial pressure of CO2

rise in active muscle tissue during exercise. The CO2 produced
by exercising muscle reacts with the water in blood to form carbonic acid, which dissociates and releases a hydrogen ion. As a
result, the pH of the blood in exercising muscle drops.
Decreases in pH alter hemoglobins conformation. These
shape changes make hemoglobin more likely to unload O2 at any
given value of tissue PO2. As FIGURE 45.16 shows, this phenomenon, known as the Bohr shift, causes the oxygenhemoglobin
equilibrium curve to shift to the right when pH declines.
The Bohr shift is important because it makes hemoglobin
more likely to release oxygen during exercise or other conditions
in which PCO2 is high, pH is low, and tissues are under oxygen
stress. Increasing temperature has the same result: It shifts the
curve to the right, representing a greater unloading of oxygen to
tissues at any given PO2.
100
pH 7.4

80
60

pH 7.2

Bohr shift

40
20
0

20

30

40

60

80

100

PO2 (mm Hg) in blood within tissue

FIGURE 45.16 The Bohr Shift Makes Hemoglobin More Likely to
Release Oxygen to Tissues with Low pH. As pH drops, oxygen
becomes less likely to stay bound to hemoglobin at all values of
tissue PO2. Exercising tissues have lower pH than resting tissues
and thus receive more oxygen from hemoglobin.