TRANSPORT OF

GASES

TRANSPORT OF OXYGEN FROM THE

LUNGS TO THE BODY TISSUES

Transport of O2 occurs due to constant circulation of blood

and diffusion of O2 in the direction of conc. gradient (pO2).

Alveolar air pO2 : 100-104 mmHg

Pulmonary arterial blood pO2 : 40 mmHg

Arterial blood pO2 : 95 mmHg

Tissue interstitial fluid pO2 : 40 mm Hg

Tissues : 5- 40 mm Hg ( avg. 23 mmHg)

Venous blood pO2 : 40 mmHg

FACTORS AFFECTING OXYGEN DELIVERY

O2 delivery to a particular tissue depends on

1.

The amount of O2 entering the lungs

2.

The adequacy of pulmonary gas exchange

3.

The blood flow to the tissue.

- The blood flow depends on the degree of constriction of the

vascular bed in the tissue and the cardiac output.

4.

The capacity of the blood to carry O2.

The amount of O2 in the blood is determined by

i. the amount of dissolved O2
ii. the amount of hemoglobin in the blood
iii. the affinity of the hemoglobin for O2

CARRIAGE OF OXYGEN IN THE

BLOOD
1.

In dissolved form :

. At

the normal arterial Po2 of 95 mm Hg, about 0.3 ml of oxygen is

dissolved in every 100 ml of water in the blood.

. When

the Po2 of the blood falls to the normal 40 mm Hg in the tissue

capillaries, only 0.12 ml of oxygen remains dissolved.

.

0.17 ml of oxygen is normally transported in the dissolved state to

the tissues by each 100 ml of arterial blood flow.

. The

amount of oxygen transported to the tissues in the dissolved

state is normally slight, only about 3 % of the total, as compared

with 97 % transported by the Hb.

2. IN COMBINATION WITH
HAEMOGLOBIN

Each of the 4 Fe in Hb can reversibly bind one O2 molecule.

The iron stays in the ferrous state, so that the reaction is

oxygenation, not oxidation.

It has been customary to write the reaction of hemoglobin

with O2 as Hb + O2 HbO2

Because it contains four deoxyhemoglobin (Hb) units, the

hemoglobin molecule can also be represented as Hb4, and it
actually reacts with four molecules of O2 to form Hb4O8.

The quaternary structure of hemoglobin determines its affinity

for O2.

In deoxyhemoglobin, the globin units are tightly bound in a

tense (T) configuration, which reduces the affinity of the
molecule for O2.

When O2 is first bound, the bonds holding the globin units are
released, producing a relaxed (R) configuration, which
exposes more O2 binding sites.

The net result is a 500-fold increase in O2 affinity.

In tissue, these reactions are reversed, releasing O2.

When blood is equilibrated with 100% O2 (PO2 = 760 mm Hg), the

normal hemoglobin becomes 100% saturated.

When fully saturated, each gram of normal hemoglobin contains

1.39 mL of O2.

The traditional figure is 1.34 mL of O2.

The hemoglobin concentration in normal blood is about 15 g/dL.

(14 g/dL in women and 16 g/dL in men).

Therefore, 1 dL of blood contains 20.1 mL (1.34 mL x 15) of O 2

bound to hemoglobin when the hemoglobin is 100% saturated.

The amount of dissolved O2 is a linear function of the PO2 (0.003

mL/dL blood/mm Hg PO2).

Because of a slight admixture with venous blood that

bypasses the pulmonary capillaries (physiologic shunt),
the hemoglobin in systemic arterial blood is only 97%
saturated.

The arterial blood therefore contains a total of about

19.8 mL of O2 per dL : 0.3 mL in solution and 19.5 mL
bound to hemoglobin.

In venous blood at rest, the hemoglobin is 75% saturated

and the total O2 content is about 15.2 mL/dL : 0.12 mL in
solution and 15.1 mL bound to hemoglobin.

Thus, at rest the tissues remove about 4.6 mL of O2 from

each deciliter of blood passing through them

In this way, 250 mL of O2 per minute is transported from

the blood to the tissues at rest.

THE OXYGENHEMOGLOBIN
DISSOCIATION CURVE

It is showing the relationship between PO2 and the % of

the Hb binding sites that are occupied by oxygen molecules
(percent saturation).

This curve has a characteristic sigmoid shape due to the TR

interconversion.

Combination of the Ist heme in the Hb molecule with O 2 increases

the affinity of the second heme for O2,

Oxygenation of the 2nd increases the affinity of the 3rd, and so on,
so that the affinity of Hb for the 4th O 2 molecule is many times that
for the first.

OXYGENHEMOGLOBIN
DISSOCIATION CURVE. PH 7.40,
TEMPERATURE 38 C

LEFT / RIGHT SHIFT OF O2-HB DISSOCIATION CURVE

A CONVENIENT INDEX FOR COMPARISON OF SUCH SHIFTS IS
THE P50

The P50 represents the partial pressure at which Hb is 50% saturated

with oxygen.
When the curve shifts to the right, the P50 & Hb affinity to O2
When the curve shifts to the left, the P50 & Hb affinity to O2

FACTORS AFFECTING THE AFFINITY OF HEMOGLOBIN FOR

OXYGEN

4 important conditions affect the oxygen

hemoglobin dissociation curve:

1.

the pH

2.

PCO2

3.

the temperature

4.

the concentration of 2,3-biphosphoglycerate

(BPG; 2,3-BPG)

FACTORS THAT SHIFT THE

OXYHEMOGLOBIN DISSOCIATION
CURVE
Foetal Hb ,
Myoglobin

Most of the unsaturation of hemoglobin that occurs in the tissues is

secondary to the decline in the PO2, but an extra 12% unsaturation is
due to the rise in PCO2 and consequent shift of the dissociation curve to
the right.

The decrease in O2 affinity of Hb when the CO2 enters blood from

tissues is called the Bohr effect .

Bohrs effect is loading of CO2 & unloading of O2 at tissue level.

The Bohr effect is caused in part by the change in pH that occurs as

CO2 increases, and in part to the direct effects of CO2 on Hb.

It is closely related to the fact that deoxygenated Hb binds H + more

actively than does oxygenated Hb .

Mature RBCs respire via anerobic glycolysis.

2,3-BPG is very plentiful in red cells. It is formed from 3phosphoglyceraldehyde, which is a product of glycolysis via the
EmbdenMeyerhoff pathway.

It is a highly charged anion that binds to the -chains of

deoxyhemoglobin.

Because acidosis inhibits red cell glycolysis, the 2,3-BPG

concentration falls when the pH is low & also in stored blood.

Conversely, thyroid hormones, growth hormones, and

androgens , anaemia , hypoxia ,exercise can all increase the
concentration of 2,3-BPG and the P50.

MYOGLOBIN

Iron containing pigment found in muscles specialized for

sustained contraction. e.x heart & leg muscles

Contains only 1 heme with 1 polypeptide chain

It takes up O2 at low pressure more readily than blood.

So ,dissociatian curve rectangular hyperbola.

Does not show Bohr effect

Acts as temporary O2 storehouse in the muscles

UTILIZATION COEFFICIENT.

The percentage of the blood that gives up its

oxygen as it passes through the tissue capillaries
is called the utilization coefficient.

The normal value for this is about 25 per cent.

During

strenuous

exercise,

the

utilization

coefficient inthe entire body can increase to 75 to

85 per cent.

CARBON DIOXIDE
TRANSPORT

CARBON DIOXIDE TRANSPORT

CO2 plays a critical role in the maintenance of

physiological homeostasis, and it is a major factor in
regulating hydrogen ion (H+) concentrations in blood,
cells, and other body tissues.

CO2 is produced at a rate of about 200 ml/min

Arterial PaCO2 depends solely on alveolar ventilation and

CO2 production.

carbon dioxide can diffuse about 20 times as rapidly as

oxygen

Transport of CO2 occurs due to constant circulation of

blood and diffusion of CO2 in the direction of conc.
gradient (pCO2).

Intracellular PCO2 : 46 mm Hg;

Interstitial PCO2 :45 mm Hg.

PCO2 of the arterial blood : 40 mm Hg (2.4 ml/dL)

PCO2 of the venous blood : 45 mm Hg (2.7 ml/dL)

PCO2 of the pulmonary arterial blood : 45 mm Hg

PCO2 of the alveolar air : 40 mm Hg.

CARRIAGE OF CARBONDIOXIDE IN
THE BLOOD (PLASMA & RBCS)

Under normal resting conditions, an average of 4 mL

of carbon dioxide is transported from the tissues to the
lungs in each 100 mL of blood.

I.

In dissolved form (0.3 ml /dL) or 7 10 %

II.

In carbamino compounds (0.7 ml /dL) or 22-23%

with Hb & Plasma proteins

III.

In bicarbonate form ( 3 ml/dL) or 68- 70 %

Binding of O2 to hemoglobin reduces its affinity for

CO2(Haldane effect).

Because the rise in the HCO3 content of red cells is much

greater than that in plasma as the blood passes through the
capillaries, about 70% of the HCO3 formed in the red cells
enters the plasma.

The excess HCO3 leaves the red cells in exchange for Cl .

This process is mediated by anion exchanger 1 (AE1;
formerly called Band 3), a major membrane protein in the red
blood cell.

Because of this chloride shift,( Hamburger shift ) the Cl

content of the red cells in venous blood is significantly greater
than that in arterial blood.

CO2 DISSOCIATION CURVES.

The dissociation (removal and uptake) of CO2 from the

blood is almost directly related to the PCO2, and
therefore the dissociation curve for CO2 is linear

The saturation of hemoglobin with O2 has a major

effect on the CO2 dissociation curve.

Although O2 and CO2 bind to hemoglobin at different

sites, deoxygenated hemoglobin has a greater affinity
for CO2 than does oxygenated hemoglobin.

The deoxygenated Hgb more readily forms carbamino

compounds, and it also more readily binds the free H +
ions that are released during the formation of HCO 3

FACTORS AFFECTING CO2

DISSOCIATION CURVE
1.

Oxy/deoxyHb

2.

DPG

3.

Temperature

RESPIRATORY EXCHANGE RATIO

The ratio of carbon dioxide output to oxygen uptake is

called the respiratory exchange ratio (R).

For a person on a normal diet consuming average amounts

of carbohydrates, fats, and proteins :

The average value for R is considered to be 0.825.