Physical Principles &

Physiology of Gas
Exchange
DR. WONG JUN LEONG, MD, M.SC.

LECTURER

FACULTY OF MEDICINE & HEALTH SCIENCES (FMHS)

UNIVERSITI TUNKU ABDUL RAHMAN (UTAR)

OUTLINE
Exchange of gases in alveoli and tissues
Partial pressures of gases
Alveolar gas pressures
Gas exchange between alveoli and blood
Matching ventilation and blood flow in alveoli
Gas exchange between tissues and blood
Transport of oxygen in blood
Effect of Po2 on hemoglobin saturation
Effects of CO2 and other factors on
hemoglobin saturation
Transport of CO2 in blood
Transport of H+ between tissues and lungs
LEARNING OUTCOME
Student should be able to:
1.  Know the effects on alveolar gas pressure
2.  Describe the Dalton and Henry laws.
3.  Describe the gas transporta?on in blood.
4.  Recognizing the Carbon Monoxide poisoning
5.  Recall the Bohr and Haldane effects
Exchange of Gases in Alveoli and Tissues
ParQal Pressures of Gases
Alveolar Gas Pressures
Gas Exchange Between Alveoli and Blood
Matching of VenQlaQon and Perfusion in Alveoli
Transport of Oxygen in Blood

Oxygen is transported
in the blood bound to
hemoglobin.
12
Oxygen-Hemoglobin DissociaQon Curve
Effect of Hemoglobin Binding to Oxygen
Oxygen Movement in Lungs and Tissues
Carbon Monoxide Poisoning
•  This is a type of hypoxemic hypoxia. It is the leading
cause of death from fire.

•  CO is an odorless, colorless gas that competes with O2 for

the binding sites on the hemoglobin. It has a 200-?mes
greater affinity for hemoglobin than O2 does.

•  The symptoms are confusion, respiratory distress, the

skin becomes cherry red. NO CYANOSIS is detectable.

•  To treat it, hyperbaric treatment or 100% oxygen is used.

Effects of
DPG and
Temperature
on Hemoglobin
SaturaQon
Effects of
Acidity and
Fetal
Hemoglobin on
Hemoglobin
SaturaQon
Transport of Carbon Dioxide in Blood
Transport of Hydrogen Ions
Between Tissues and Lungs
 HOMETASK
1.  Revise the block 1 lecture.
2.  Outline the similari?es and differences between myoglobin and
adult haemoglobin, explaining the physiological relevance of the
differences.
3.  Explain how oxygen supply of organs is maintained during
isovolaemic haemodilu?on.
2. Outline the similariQes and differences between
myoglobin and adult haemoglobin, explaining the
physiological relevance of the differences.
 Func%on
 Hb: Oxygen carriage → lungs to ?ssues, CO₂ carriage, Acid-base buffer
 Myoglobin: Oxygen Store → for exercising muscle
 Loca%on
 Hb is located in large concentra?ons (≈15g/L) in red blood cells that
circulate throughout the blood stream.
 Myoglobin is a haem containing pigment protein found in skeletal and
cardiac muscle.
 Myoglobin is only found in the blood stream when it is released following
muscle injury → abnormal finding (↑ in AMI or rhabdomyolysis)
 Myoglobin is toxic to renal tubular epipthelium and large amounts of
myoglobin (eg in rhabdomyolysis) can cause renal failure.
  Structure
 Haemoglobin and Myoglobin are structurally related. Both are globular
proteins and both contain a haem moiety which binds O₂.
 Haem is an protoporphryin ring deriva?ve with a central Fe2+ molecule that
binds O₂
 Haemoglobin:
 Hb contains 65-70 % of total body iron
 Globular molecule made up of four subunits, each containing a haem
moiety conjugated to a polypep?de.
 Polypep?des collec?vely = globin → two pairs 2α + 2β → 4 haem moie?es
 Can bind a total of 4 Hb and also exhibits coopera?ve affinity (each
subsequent O₂ binding takes less energy → sigmoid shaped OHDC
 Myoglobin:
 Myoglobin contains 4-5 % of total body iron
 Myoglobin is a single-chain globular protein containing a single haem
moiety
 Unlike haemoglobin it does not exhibit coopera?ve affinity when binding
oxygen since it does not exist in a tetramer forma?on → its dissocia?on
curve is a rectangular hyperbola rather than a sigmoid curve.
 Carriage Of O₂
• Hb: Sigmoid shaped dissocia?on curve, P50 26.6mmHg,
opera?ng range 100-20mmHg
•  Hb has to carry oxygen from the lungs (PaO2 100) down the 'oxygen
cascade' to the ?ssues. P50 suits this opera?ng range and enables
appropriate loading and unloading of O2.
• Myoglobin: Rectangular hyperbole dissocia?on curve, P50
2.75mmHg, opera?ng range 5-1mmHg
•  Myoglobin needs to have a P50 less than Hb so it can take up O₂ from it.
•  Myoglobin needs to be able to load and unload O₂ in the range of pO2
values that occur within the cell → it’s p50 of 2.75mmHg is well matched to
the intracellular opera?ng range of pO2 (1↔5mmHg)
•  The myoglobin content is greatest in muscles specialized for sustained
contrac?on → the muscle blood supply is open compressed during such
contrac?ons and myoglobin may provides O₂ when blood flow is cut off.
3. Explain how oxygen supply of organs is
maintained during isovolaemic
haemodiluQon
v Increased cardiac output
and blood flow generally.
v Increased ?ssue perfusion.
v Increased (maintained) O2
delivery at the ?ssue.