7.1-7.6 Mass Transport Flashcards
When is mass transport used?
Over large distances, efficient movement of substance to and from exchange surfaces
What type of structure does haemoglobin have?
Quaternary structure - four polypeptides each associated with a haem group (4 oxygens can be carried by a single molecule)
What type of protein is haemoglobin and why is it soluble?
Globular protein
Curled up - hydrophilic side chains face outwards (soluble) and hydrophobic side chains face inwards (maintain structure)
Therefore soluble and good for transport in the blood
What are the haemoglobins?
A group of chemically similar molecules found in many different organisms
What is the process by which haemoglobin binds with oxygen?
Loading or associating
Takes place in lungs
What is the process by which haemoglobin releases its oxygen? Where does it take place?
Unloading or dissociating
Takes place in the tissues
What does a high affinity (chemical attraction) mean?
Take up oxygen more easily
Release it less easily
What does a low affinity mean?
Take up oxygen less easily
Release it more easily
What is the role of haemoglobin?
Transport oxygen (oxygen is not soluble)
What must haemoglobin do to efficiently transport oxygen? How does it do this?
Readily associate with oxygen at the surface where gas exchange takes place
Readily dissociate from oxygen at those tissues requiring it
Changes shape in the presence of certain substances
How does oxyhaemoglobin form?
Prosthetic haem group contains Fe2+ which combines reversibly with an oxygen molecule, forming oxyhaemoglobin
Why are there different haemoglobins?
Shape of the molecule
Different shape so there is a different affinity for oxygen
What is the oxygen dissociation curve?
The rate at which oxygen associates, and also dissociates, with haemoglobin at different partial pressures of oxygen (pO2)
What is partial pressure?
The pressure exerted by oxygen within a mixture of gases; it is a measure of oxygen concentration
Explain the shape of the oxygen dissociation curve
- The shape of the haemoglobin molecule means it is difficult for the first oxygen molecule to bind to haemoglobin –> binding of the first oxygen occurs slowly, (relatively shallow curve at the bottom left corner of the graph)
- After the first oxygen molecule binds to haemoglobin, the haemoglobin quaternary shape changes so it is easier for the next haemoglobin molecules to bind which speeds up binding of the remaining O2 (steeper part of the curve in the middle of the graph)
- As the haemoglobin molecule approaches saturation it takes longer for the fourth O2 to bind due to the shortage of remaining binding sites (levelling off of the curve in the top right corner of the graph)
What is cooperative binding?
The shape change of haemoglobin leading to easier oxygen binding
What does it mean if the curve is further to the left?
The greater is the affinity of haemoglobin for oxygen (it loads oxygen readily but unloads it less easily)
What does it mean if the curve is further to the right?
The lower is the affinity of haemoglobin for oxygen (so it loads oxygen less readily but unloads it more easily)
What is the Bohr effect?
Haemoglobin has a reduced affinity for oxygen
Greater conc of CO2, more readily the haemoglobin release its oxygen
Explain the behaviour of haemoglobin at the lungs (gas-exchange surface) due to carbon dioxide concentration
- Conc. of CO2 is low because it diffuses across the exchange surface and is excreted from the organism
- Affinity of haemoglobin for oxygen is increased (high conc of O2 in lungs) so oxygen is readily loaded by haemoglobin
- Reduced CO2 has shifted the oxygen dissociation curve to the left
Explain the behaviour of haemoglobin at rapidly respiring tissues (eg muscles) due to carbon dioxide concentration
- Conc of CO2 is high
- Affinity of haemoglobin for oxygen is reduced (low conc of oxygen in muscles) oxygen is readily unloaded from the haemoglobin into the muscle cells
- Increased CO2 has shifted the oxygen dissociation curve to the right
Describe how oxygen is loaded, transported and unloaded in the blood
- Haemoglobin carries oxygen/has a high affinity for oxygen
- In red blood cells
- Loading of oxygen takes place in the lungs at high partial pressure
- Unloads oxygen to respiring cells or tissues at low partial pressure
- Unloading due to higher carbon dioxide concentration
Why do different species have different types of haemoglobin?
Adapted to their environment so their haemoglobin has different oxygen transport properties
- Less O2 in environment = high affinity haemoglobin
- High metabolic rate = haemoglobin with a low affinity for O2 so that O2 released more easily at the respiring tissues
- Type of Hb relies on the environment and metabolism of the organism
What is myoglobin and its uses?
Conjugated protein (similar to haemoglobin)
Stores O2 in the muscles
Left of haemoglobin so has a high affinity for oxygen
Only releases oxygen when pO2 is low eg during exercise