Gas transport:
Oxygen transport
Dr. S.B.Deshpande
Professor of Physiology
Kanchanbari, Biratnagar,
Nepal
RESPIRATORY SYSTEM TOTAL=16 classes
1- Functional anatomy of respiratory system 1
2- Mechanism and mechanics of breathing-I 1
3- Mechanism and mechanics of breathing-II 1
4- Mechanism and mechanics of breathing-III 1
5- Pulmonary function tests 1
6- Pulmonary circulation & gas exchange-I 1
7- Pulmonary circulation & gas exchange-II 1
8- Pulmonary circulation & gas exchange-III 1
9- Gas transport-I 1
10-Gas transport-II 1
11-Regulation of respiration-I 1
12-Regulation of respiration-II 1
13-Respiration in unusual environment-I 1
14-Respiration in unusual environment-II 1
15-Principles of artificial respiration 1
16-Applied respiratory physiology 1
Gas Transport-1 (as prescribed by KU)
• O2 transport- factors influencing the combination
of hemoglobin with Oxygen
• Oxygen dissociation curve: plot, features,
physiological advantage and its shape
• Factors affecting the O2-Hb dissociation curve, shift
of the curve, Bohr effect
• CO transport and its effects
Transport of gases and Blood pH
• O2 transport- lungs (pulmonary vein to systemic
arteries)
• CO2 transport- tissues to veinous circulation-right
side of heart- pulmonary artery for release
• Acid base balance & Blood pH
O2 transport
• Dissolved form
• Combination with Hb
Dissolved O2
• Obeys Henry’s law- the “solubility of a gas in a solution is
proportional to the pressure gradient it exerts” C = kP.
• Dissolved O2- 0.003 ml/mmHg/100 ml of blood.
• Normal arterial blood with a PO2 of 100 mm Hg contains 0.3
ml O2/100 ml and the venous blood have 0.12 ml/dL of O2.
• Thus dissolved O2 transported in the blood is totally
inadequate
• Resting O2 consumption is 250ml/min comes from 5 L blood
with AV O2 difference is 5 ml/dl.
• However, the tissue requirements may be as high as 3L/min O2
(VO2max)
• Clearly, an additional method of transporting O2 is required.
Total O2 in the blood
• The amount of O2 in the blood is determined by
• Dissolved O2,
• With hemoglobin in the blood,
• The affinity/availability of hemoglobin for O2.
Hb a carrier of O2
• Hemoglobin is a protein made up of four subunits, each of which contains a
heme moiety attached to a polypeptide chain.
• In normal adults, hemoglobin molecules contain 2α and2β chains. (HbA)
Heme is a porphyrin ring complex that includes one atom of ferrous iron.
• Each of the four iron atoms in hemoglobin can reversibly bind one O2
molecule. The iron stays in the ferrous state, so that the reaction is
oxygenation (not oxidation).
• The reaction of hemoglobin with O2 as
1. Hb + O2 ⇄ HbO2. - Releases the tense state
2. HbO2+ O2 ⇄ Hb2O4. - Relaxed
3. Hb2O4 + O2 ⇄ Hb3O6.
4. Hb6 + O2 ⇄ Hb8O2.
• Thus Hb reacts with 4 molecules of O2 to form Hb4O8 within 0.01 s reverse
also happens in the same speed.
Hemoglobin molecule Adult Hb- HbA-
• Has 2 2 chains
• Has < affinity than HbF
• Responsive to 2,3 BPG
• Forms acid/alkali hematin
• 95 % in adults
Fetal Hb- HbF-
heme
• Has 2 2
• Affinity for O2
• Less responsive to 2,3 BPG
• Alkali resistant
• Shifts O2 curve to Lt
HbS-substitution of valine for glutamic acid at HbA2- 2 2 - 2-3% in adults
6th position of the β globin-genetic defect >> in thalassemia
Oxygenation of Hb
Oxyhemoglobin dissociation curve
Oxyhemoglobin dissociation curve
1. Hb + O2 ⇄ HbO2.
2. HbO2+ O2 ⇄ Hb2O4
3. Hb2O4 + O2 ⇄ Hb3O6
4. Hb6 + O2 ⇄ Hb8O2
Affinity of O2 increases
at each stage
Saturation = (O2
combined with Hb/Total
02 capacity)X 100
P50 value -
PO2 required for 50
% saturation of Hb
Indicates O2 affinity
With HbA it is
about 26 mmHg
Increased in
• PCO2
• H+
• Temp
• 2,3 BPG
• All exercise
Bohr effect
• The decrease in O2 affinity of hemoglobin when the pH of
blood falls iscalled the Bohr effect
• Because deoxygenated hemoglobin (deoxyhemoglobin) binds
H+ more actively than does oxygenated hemoglobin
(oxyhemoglobin).
• The pH of blood falls as its CO2 content increases, so that
when the PCO2 rises, the curve shifts to the right and the P50
rises.
• Most of the unsaturation of hemoglobin that occurs in the
tissues is secondary to the decline in the PO2, but an extra 1–
2% unsaturation is due to the rise in PCO2 and consequent
shift of the dissociation curve to the right.
2,3-DPG or BPG
• 2,3-DPG is very plentiful in red cells. It is formed from 3-
phosphoglyceraldehyde, which is a product of glycolysis via the
Embden–Meyerhof pathway.
• It is a highly charged anion that binds to the β chains of
deoxyhemoglobin.
• One mole of deoxyhemoglobin binds 1 mol of 2,3-DPG. Thus
unloads O2
• Acidosis decreases 2,3 DPG-
• Thyroid, GH, Androgens Increase 2,3BPG
• Stored blood of blood bank-depletes 2,3 BPG
Effect of CO and Anemia on Hb dissociation curve
CO toxicity
• CO + Hb- COHb
• CO has about 240 times > affifinity othan O2 for Hb;
• Thus PCO- 240 times lower to achieve the same magnitude of Saturation
• The CO dissociation curve is almost identical in shape to the O2
dissociation curve but at lower pressures
• For example
– At 40 mmHg PO2- SO2 is 75 %
– Similarly at 0.16 mmHg (40/240) of PCO about 75% of the Hb is combined
with CO
• Binding of CO is stronger hence not allows O2 to bind with Hb
• In the presence of COHb also shifts the O2 dissociation curve to the left,
thus interfering with the unloading of O2.
• Hyperbaric O2 is required to displace CO
Dissociation curves for hemoglobin and myoglobin
• Myoglobin resembles hemoglobin but
binds 1 rather than 4 mol of O2 per
mole protein.
• Lack of cooperative binding – showing a
rectangular hyperbola than sigmoid
curve
• MbO2- leftward shift-indicating higher
affinity for O2,
• O2 is released only at low PO2 values
(eg, during exercise).
• The myoglobin content is greatest in
muscles specialized for sustained
contraction-slow muscles
• Reduced blood supply thus myoglobin
continue to provide O2 under reduced
blood flow and/or reduced PO2 in the
blood.
Next class
We will continue with the
Transport of CO2
Thank you
