3B: Mass transport Flashcards
Describe 3 adaptations of red blood cells
- Biconcave shape = maximises SA for gas exchange
- Small + flexible = to pass through narrow capillaries (pressed to the sides to maximise gas exchange)
- No nucleus = more room to carry respiratory gases
What is the function of red blood cells?
To transport O₂ around the body
How does haemoglobin allow RBCs to carry respiratory gases (especially oxygen)
- It has an affinity for oxygen (can carry up to 4 O2 molecules)
- Oxygen binds to the ‘haem’ Fe2 + group of haemoglobin
What is haemoglobin called when it becomes oxygenated?
Oxyhaemoglobin
What are the haemoglobins?
- The haemoglobins are a group of chemically similar molecules found in many different organisms.
- They are protein molecules with quaternary structures
Describe the primary structure of a haemoglobin molecule.
Sequence of amino acids in the 4 polypeptide chains
Describe the secondary structure of a haemoglobin molecule.
Each of the 4 polypeptide chains is coiled into a helix
Describe the tertiary structure of a haemoglobin molecule.
Each polypeptide chain is folded into a precise shape
Why is the tertiary structure of a haemoglobin molecule so important?
- The tertiary structure of a protein determines the 3D shape of the protein
- For haemoglobin this is an important factor in its ability to carry oxygen
Describe the quaternary structure of a haemoglobin molecule.
- All 4 polypeptides are linked together to form an almost spherical molecule
- Each polypeptide is associated with a haem group
What does each haem group, in haemoglobin, contain?
Each haem group contains a ferrous group (Fe2+) ion
- Each iron ion can combine with a single oxygen molecule
= a total of 4 O2 molecules can be carried
In humans, where does the loading/ associating of haemoglobin & oxygen take place?
In the lungs
In humans, where does the unloading/ dissociating of haemoglobin & oxygen take place?
In the tissues
What is the process by which haemoglobin binds with oxygen called?
Loading/ associating
What is the process by which haemoglobin releases its oxygen called?
Unloading/ dissociating
What is the role of haemoglobin?
To transport oxygen from gas exchange surafces to respiring tissues
To be efficient at transporting oxygen, haemoglobin must:
- Readily associate with oxygen at the surface where gas exchange takes place
- Readily dissociate from oxygen at those tissues requiring it
What adaptation allows haemoglobin to readily associate + dissociate from oxygen in different environments?
The fact that haemoglobin can change its affinity for oxygen under different conditions.
How does haemoglobin change its affinity for oxygen in different environments?
Because its shape changes in the presence of certain substances, e.g carbon dioxide
Describe what happens to haemoglobin in respiring tissue.
- In respiring tissue there’s a high CO₂ conc. and a low O₂ conc.
- In the presence of carbon dioxide, the new shape of the haemoglobin molecule binds more loosely to oxygen
- It has a low affinity for O₂
= resulting in the haemoglobin unloading its oxygen
Describe what happens to haemoglobin at the gas exchange surface.
- At the exchange surface there’s a high O2 conc. and a low CO2 conc.
- This means that the haemoglobin will have a high affinity for O2
= resulting in the haemoglobin loading its oxygen
Why do different hemoglobins have different affinities for oxygen?
Due to the shape of the molecule
Why do different organisms have haemoglobins with different shapes - and therefore oxygen affinities?
- Because each species produces a haemoglobin with a slightly different amino acid sequence
- Therefore the haemoglobin of each species will have a different tertiary + quaternary structure
= and hence different oxygen binding properties
What is the partial pressure of oxygen (PO2) referring to?
The amount of oxygen in the tissue
What is PO2 measured in?
kPa
What is the graph that shows the relationship between the saturation of haemoglobin + O2 and the PO2 known as?
The oxygen dissociation curve
What shape is the graph that shows the relationship between the saturation of Hb + O2 and the PO2 known as?
An S-shape
Why is the oxygen dissociation curve shallow initially?
- The shape of the Hb molecule makes it difficult for the first O2 molecule to bind to 1 of the sites on its 4 polypeptide subunits because they are closely united
- Therefore in low O₂ conc.s little O₂ binds to Hb
What does Hb refer to?
Haemoglobin
How does the binding of the 1st O2 change the hemoglobins structure?
- The binding of the first O₂ changes the quaternary structure of the Hb molecules
- Which causes it to change shape
- This change makes it easier for the other subunits to bind to an O₂ molecule
Why does the gradient of the oxygen dissociation curve then steepen?
Hint: positive cooperativity
- After the 1st O2 binds, it takes a smaller increase in the PO2 to bind the 2nd oxygen molecule than it did to bind the 1st one.
- This is known as positive cooperativity because the binding of the first molecule makes it easier for the next one and so on.
Why does the gradient of the oxygen dissociation curve reduce and flatten off?
- After the binding of the 3rd oxygen, the probability of the last binding site being filled is lower
- This is because with the majority of the binding sites occupied, it is less likely that a single oxygen molecule will find an empty site to bind to
The further to the left the curve, the _______ is the affinity of Hb for oxygen.
The further to the left the curve, the greater is the affinity of Hb for oxygen.
What does it mean for the haemoglobin molecule if it has a high affinity for oxygen?
It means it will load oxygen readily but will unload it less easily
What does it mean for the haemoglobin molecule if it has a low affinity for oxygen?
It means it will load oxygen less readily but will unload it more easily
The further to the right the curve, the _____ is the affinity of Hb for oxygen.
The further to the right the curve, the lower is the affinity of Hb for oxygen.
What is carbon dioxides effect on haemoglobin’s affinity for oxygen?
In the presence of CO2, Hb has a reduced affinity for O2
- The greater the conc. of CO2 the more readily the Hb releases its oxygen (The Bohr effect)
Describe the behaviour of haemoglobin at the gas exchange surface (e.g lungs)
- Low conc. of CO2
- High conc. of O2
- The affinity of Hb for O2 is increased
= O2 is readily loaded by haemoglobin - The reduced CO2 conc. has shifted the oxygen dissociation curve to the left
Why is the conc. of carbon dioxide low at the gas- exchange surface (e.g lungs)
The conc. of CO2 is low because it diffuses across the exchange surface and is excreted from the organism
Describe the behaviour of haemoglobin in rapidly respiring tissues
- High conc. of CO2
- Low conc. of O2
- The affinity of Hb for O2 is reduced
= O2 is readily unloaded from the Hb into the muscle cells - The increased CO2 conc. has shifted the oxygen dissociation curve to the right
Why does the greater the CO2 conc. mean the more readily Hb will unload O2?
This is because dissolved carbon dioxide is acidic and the low pH causes Hb to change shape
What is the pH like at the gas exchange surface? What does this mean for Hb and oxygen loading?
- The pH is slightly raised due to the low conc. of carbon dioxide
- The higher pH changes the shape of Hb into one that enables it to load oxygen readily
- This shape also increases the affinity of Hb for oxygen, so it’s not released while being transported in the blood to the tissues
What is the pH of carbon dioxide in solution like?
It is acidic (low pH)
What is the pH of the blood within the respiring tissues like?
- CO₂ is acidic in solutions
- So the pH of the blood within the tissues is lowered
How does a lower pH (in respiring tissues) effect haemoglobin?
Lower pH changes the shape of Hb = lowers affinity for O₂
- Therefore Hb unloads O₂ into the respiring tissues
Explain how: the more active a tissue, the more oxygen is unloaded.
The higher the rate of respiration –> the more CO2 the tissues produce –> the lower the pH –> the greater the Hb shape change –> the more readily the O2 is unloaded –> the more O2 is available for respiration
In humans, where does haemoglobin become saturated with oxygen?
When it passes through the lungs
What is the overall saturation of haemoglobin at atmospheric pressure? Why?
97%
- Not all Hb molecules are loaded with their maximum 4 oxygen molecules
When haemoglobin reaches a tissue with a low respiratory rate, how many oxygen molecules will be released?
Only 1 oxygen will normally be released
After reaching a tissue with a low respiratory rate, what will the oxygen % of the blood (containing haemoglobin) returning to the lungs be like?
The blood returning to the lungs will therefore contain Hb that is still 75% saturated with oxygen
If tissue is very active, how many oxygen molecules are normally unloaded?
3 oxygen molecules will usually be unloaded from each Hb molecules
How have some organism’s haemoglobin molecules evolved to live in an environment with a low PO2?
- Animals that live in an environment with a lower PO2 have evolved haemoglobin that has a higher affinity for oxygen
- Compared to the haemoglobin of animals that live where the PO2 is higher
What is the oxygen dissociation curve of a lugworms haemoglobin like? What does this mean?
- The dissociation curve is shifted far to the left of that of a human
- This means that the haemoglobin of the lugworm is fully loaded with oxygen even when there if little available in its environment
How are llamas adapted to their environment?
Answer in relation to its haemoglobin
- Llamas live at high altitudes = the atmospheric pressure is lower and so is the PO2
- It is therefore difficult to load haemoglobin with oxygen
- Llamas have a type of haemoglobin that has a higher affinity for oxygen than human haemoglobin
- The oxygen dissociation curve will shift to the left of human Hb
What happens to the SA:V when the size of the organism increases?
The SA:V decreases
Why are specialised exchange surfaces required for larger organisms?
- Because as the size of an organism increases it’s SA:V decreases
- SA:V decreases to a point where the needs of the organism cannot be met by the body surface/ diffusion alone
The lower the SA:V the _____ active the organism, the _____ is the need for a more __________ transport system with a ____.
The lower the SA:V the More active the organism, the Greater is the need for a more Specialised transport system with a Pump.
Give an example of a suitable medium used in many organisms transport systems to carry materials.
Blood
Why is the suitable transport medium in may organisms transport systems water based?
- Suitable mediums are normally a liquid based on water
- This is because water readily dissolves substances
- Also water can be moved around easily, as it can also be a gas (e.g air breathed out of the lungs)
What is a common feature of transport systems, relating to it being a closed and tubular?
Commonly transport systems are:
- Closed
- Consisting of tubular vessels that contain the transport medium and forms a branching network to distribute it to all parts of the organism