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The Transport of Respiratory Gases

A major function of blood in animals is the transport of the gases oxygen and carbon dioxide, to and from respiring tissues The solubility of oxygen in water is relatively low, but the oxygen-carrying capacity of the blood in many animals is significantly increased by the presence of blood pigments Haemoglobin is a pigment found in many animals. It loads oxygen where O2 concentrations are high and unloads the gas when oxygen concentrations are low e.g. at the respiring tissues

Haemoglobin is a conjugated protein that displays quaternary structure. There are four globin polypeptide chains in each molecule. There is a haem group associated with each polypeptide chain. The haem group contains an iron atom which binds with a single molecule of oxygen.

Each haemoglobin molecule combines with four molecules of oxygen in four, separate reversible reactions The combination of the first haem group with an oxygen molecule makes it easier for a second oxygen molecule to bind to the second haem group and so on. This explains the behaviour of haemoglobin when subjected to environments of differing oxygen concentration (as shown by the sigmoidal dissociation curve)

The Oxygen Dissociation Curve

The oxygen dissociation curve for haemoglobin shows the behaviour of haemoglobin when subjected to differing partial pressures (concentrations) of oxygen The dissociation curve is sigmoidal (S-shaped) and shows the percentage saturation of haemoglobin with oxygen at varying oxygen concentrations (partial pressures)

Oxygen Tension (kPa)

0 1.3 2.6 3.9 5.3 6.6 7.9 9.3 10.5 11.8

% Saturation of Haemoglobin with Oxygen (CO2 Tension = 5.3 kPa)

0 7 27 53 70 80 87 92 96 99

The data in the table shows the percentage saturation of human haemoglobin at different oxygen tensions; use this data to construct an oxygen dissociation curve

In human lungs, the partial pressure of oxygen is around 13 kPa, and haemoglobin readily loads with oxygen (about 99% saturated) Haemoglobin remains almost saturated at partial pressures ranging from 10 to 13 kPa At partial pressures below 6 kPa, relatively large amounts of oxygen are released from oxyhaemoglobin for relatively small changes in the partial pressure of oxygen In the tissue fluids, the partial pressure of oxygen varies from 0.7 to 5.5 kPa, and the steep part of the curve coincides with these values; haemoglobin readily unloads oxygen when it encounters oxygen tensions typical of those found at the tissues of the body

Haemoglobin has a high affinity for oxygen and readily loads with oxygen at respiratory surfaces and unloads its oxygen at the tissues

When haemoglobin loads with oxygen, oxyhaemoglobin

forms

Oxyhaemoglobin unloads oxygen at the tissues.

The loading and unloading tensions are the oxygen concentrations at which haemoglobin is 95% and 50% saturated respectively
The steep part of the curve coincides with the normal working range within an organism

Loading tension is the oxygen tension at which 95% of the haemoglobin molecules are saturated Unloading tension is the oxygen tension at which 50% of the haemoglobin molecules are saturated

The Bohr Shift

For many animals, the dissociation curve for haemoglobin is influenced by temperature, pH and carbon dioxide concentration An increase in temperature, acidity (lowering of pH) and carbon dioxide concentration, displaces the curve to the right and this effect is called the Bohr shift The significance of the Bohr shift is that it helps the delivery of oxygen to respiring tissues

Oxygen Tension (kPa)

0 1.3 2.6 3.9 5.3 6.6 7.9 9.3 10.5 11.8

% Saturation of Haemoglobin with Oxygen CO2 Tension (5.3 kPa)

0 7 27 53 70 80 87 92 96 99

CO2 Tension (9.3 kPa)

0 4 15 35 58 73 82 89 94 99

Use the data provided in the table to construct oxygen dissociation curves for the two different carbon dioxide concentrations; explain the effect of increasing CO2 concentration on the behaviour of haemoglobin

This increased CO2 tension forces haemoglobin to give up an additional 15% of its bound oxygen at the tissues

15%

When the carbon dioxide concentration is increased, the dissociation curve shifts to the right; this is known as the Bohr Shift

respiring tissue

With increasing concentration of carbon dioxide from pCO2 = 5.3 kPa to pCO2 = 10.7 kPa, the dissociation curve moves progressively to the right

The Significance of The Bohr Shift

Blood carbon dioxide concentrations, temperature and acidity rise when metabolic activity at the tissues increases When metabolic activity at the tissues increases, there is a greater demand for oxygen (tissue respiration is utilising oxygen at a faster rate); during muscular exercise, a local increase in temperature and CO2 concentration occurs These factors result in a localised Bohr shift such that the active tissues receive an increased supply of oxygen

Different Forms of Haemoglobin

Different forms of haemoglobin have evolved within the animal kingdom. These are related to the environmental conditions in which animals live; e.g. altitude, temperature and oxygen availability vary in different environments. Different forms of haemoglobin can also be found within the same species and generally relate to different stages in the life cycle; e.g. the human foetal haemoglobin differs from that of the adult of the species, helping the foetus to maximise its oxygen uptake

Different Forms of Haemoglobin

The forms of haemoglobin found throughout the animal kingdom differ with respect to their affinity for oxygen and this affects the shape and positioning of the oxygen dissociation curve

Different Forms of Haemoglobin

Different haemoglobin dissociation curves are generally compared to that of a typical human and the following interpretations are made: Dissociation curves that are displaced to the right indicate that affinity of the haemoglobin for oxygen is decreased. (Hb Z) This means unloading or delivery of oxygen to the tissues is increased. Oxyhaemoglobin is more likely to release its oxygen

Different Forms of Haemoglobin

Dissociation curves that are displaced to the left (Hb X) indicate that affinity of the haemoglobin for oxygen is increased, therefore unloading or delivery of oxygen to the tissues is decreased

Foetal Haemoglobin

Human foetal haemoglobin differs in structure from that of the adult The significance of this difference is to enable the transfer of oxygen from maternal to foetal blood

Oxygen Tension (kPa)

0 0.5 1.0 2.0 3.0 4.0 6.0 8.0 10.0 12.0

% Saturation of Haemoglobin with Oxygen Foetal

0 7 14 28 46 64 86 95 98 98

Maternal
0 4 8 18 30 47 79 92 97 98

Use the data provided in the table to construct dissociation curves for maternal and foetal haemoglobin; explain the advantage to the foetus of possessing a different form of haemoglobin

Foetal haemoglobin displays a dissociation curve to the left of that of the mother; the affinity for oxygen is therefore greater than that of maternal haemoglobin enabling transfer of oxygen across the placenta

The Llama lives at high altitude in the Andes of South America. The low partial pressures of oxygen has favoured the evolution of a form of haemoglobin with a high affinity for oxygen. This enables the Llamas blood to load oxygen at the low pressures that prevail in its environment

Oxygen Tension (kPa)

0 0.5 1.0 2.0 3.0 4.0 6.0 8.0 10.0 12.0

% Saturation of Haemoglobin with Oxygen Llama

0 6 12 30 56 77 92 97 98 98

Human
0 4 8 18 30 47 79 92 97 98

Use the data provided in the table to construct dissociation curves for the Llama and Human (for comparison); explain how the shape of the Llama dissociation curve enables this mammal to survive at high altitude

The dissociation curve for Llama haemoglobin is located to the left of that for humans (and the usual range for mammals). This higher affinity of Llama haemoglobin for oxygen adapts this mammal to high altitude environments where oxygen pressures are low

Myoglobin is a respiratory pigment found in vertebrate muscle where it functions as an oxygen store; unlike haemoglobin, this molecule consists of a single polypeptide chain with one haem group and displays a higher affinity for oxygen than the haemoglobin molecule

Myoglobin becomes saturated with oxygen at lower oxygen tensions than haemoglobin and rapidly releases oxygen when oxygen tensions fall to low levels During strenuous exercise, when the oxygen supply in the blood is unable to meet the demands of muscle tissue, myoglobin unloads its oxygen store allowing muscle contraction to continue efficiently

Myoglobin
Oxygen Tension (kPa)
0 0.5 1.0 2.0 3.0 4.0 6.0 8.0 10.0 12.0

% Saturation of Haemoglobin with Oxygen Myoglobin

0 24 46 80 90 95 96 96 96 96

Haemoglobin
0 4 8 18 30 47 79 92 97 98

Use the data provided in the table to construct dissociation curves for myoglobin and haemoglobin

Myoglobin has a higher affinity for oxygen than haemoglobin. It rapidly releases its oxygen when oxygen tensions fall to low levels. It functions as a very efficient oxygen store for muscle metabolism

Carbon Dioxide Transport

The carbon dioxide, released from the respiring tissues, is transported in the blood in three main ways:
5% is carried in simple solution in the plasma as carbonic acid 10% is carried in combination with haemoglobin; carbon dioxide combines with amino acids in haemoglobin to form carbamino-haemoglobin 85% is transported in the plasma as hydrogen carbonate ions (HCO3-)

Carbon dioxide reacts with water to form a weak acid called carbonic acid

Weak acids partially dissociate in solution and the reaction is reversible (the direction depending upon the relative concentrations of the acid and its ions); carbonic acid dissociates into hydrogen ions and hydrogen carbonate ions (HCO3-)

Carbon dioxide reacts with amino acids in the haemoglobin molecule to form carbamino haemoglobin

5%

Carbon dioxide, produced by the respiring tissues, diffuses into the local blood capillaries; 5% of the released CO2 is carried in simple solution in the plasma

5%

10% of released CO2

95% of the released carbon dioxide enters the red blood cells where 10% of the CO2 combines with haemoglobin to form carbamino haemoglobin

5%

10% of released CO2 carbonic anhydrase

85% of the released carbon dioxide rapidly combines with water in the red cells due to the presence of the enzyme carbonic anhydrase; the product of this reaction is carbonic acid

5%

10% of released CO2 carbonic anhydrase

dissociation

Once formed, carbonic acid dissociates into hydrogen ions (H+) and hydrogen carbonate ions (HCO3-)

5%

85% of the CO2 released from the tissues travels in the plasma as HCO3-

10% of released CO2 carbonic anhydrase

dissociation diffusion

As the concentration of HCO3- ions increases, HCO3ions diffuse out of the red cells down a concentration gradient

5%

85% of the CO2 released from the tissues travels in the plasma as HCO3-

10% of released CO2 carbonic anhydrase

dissociation diffusion

chloride shift

The outward flow of negative ions would disturb the electrical neutrality of the red cells if this were not offset by the inward diffusion of chloride ions (chloride shift)

5%

10% of released CO2 carbonic anhydrase

oxyhaemoglobin accepts H+, and O2 is displaced oxygen diffuses into the tissues dissociation

85% of the CO2 released from the tissues travels in the plasma as HCO3-

diffusion

chloride shift

Oxyhaemoglobin is a strong base and accepts some of the hydrogen ions (H+) formed from the dissociation of carbonic acid (HCO3-); haemoglobin is acting as a buffer, and as oxyhaemoglobin attracts hydrogen ions, oxygen is displaced and diffuses into the tissues

Events at The Alveoli of The Lungs

The reactions that occurred at the tissues are reversed at the high oxygen tensions present in the lungs Oxygen diffuses from the alveoli into the red cells where it combines with haemoglobinic acid; this releases the hydrogen ions that became bound to haemoglobin at the tissues The free hydrogen ions combine with hydrogen carbonate ions present both in the red cells and the plasma; this reaction is very rapid in the red cells due to the presence of carbonic anhydrase The carbon dioxide and some of the water, formed from these reactions, diffuse out of the blood and into the alveoli of the lungs from where they are excreted

Acknowledgements

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