Section 3 - Mass transport Flashcards
(113 cards)
What are the haemoglobins?
- Group of - Chemically similar molecules
- Protein molecules
- Quaternary structure
- To make it efficient at loading oxygen under one set of conditions but unloading it under a different set of conditions.
What makes up the structure of a haemoglobin molecule?
- Primary structure 0 sequences of amino acids in 4 polypeptide chains
- Secondary structure - the polypeptide chains are coiled into a helix
- tertiary structure - folded into a precise shape - an important factor in its ability to carry oxygen.
- Quaternary structure - 4 polypeptides linked together forming almost spherical molecule. Associated with haem group.
Which structure of the haemoglobin molecule is important in its ability to carry oxygen?
The tertiary structure as each of the polypeptide chains is folded into a precise shape.
What is the quarternary structure of a haemoglobin molecule?
- All four polypeptides are linked together to form an almost spherical molecule.
- Each polypeptide is associated with a haem group
- Ferrous (FE2+) ion.
- Each FE2+ ion can combine with a single oxygen molecule (O2)
- Product -four O2 molecules that can be carried by a single haemoglobin molecule in humans.
What is loading in the context of haemoglobin molecules?
The process by which haemoglobin binds with oxygen.
AKA associating.
In humans this takes place in the lungs
What is unloading in the context of haemoglobin molecules?
The process by which haemoglobin releases its oxygen.
AKA dissociating.
In humans this takes place in the tissues.
What does it mean if haemoglobin has a high affinity for oxygen?
Takes up oxygen more easily but releases it less easily.
What does it mean if haemoglobin has a low affinity to oxygen?
Takes up oxygen-less easily but releases it more easily.
What is the role of haemoglobin?
To transport oxygen.
In order for haemoglobin molecules to be efficient at transporting oxygen, what functions must they have?
- Readily associate with oxygen at the surface where gas exchange takes place
- readily dissociate from oxygen at those tissues requiring it.
How is it possible for haemoglobin molecules to easily load and unload oxygen molecules at similar rates of efficiency?
- It changes its affinity (chemical attraction) for oxygen under different conditions.
- Shape changes in the presence of certain substances, such as carbon dioxide.
- Presence of CO2 (Higher conc in respiring tissue), new shape of haemoglobin binds more loosely to oxygen.
- As result haemoglobin releases its oxygen.
Explain the affinity of haemoglobin for oxygen in on a gas exchange surface
- High O2 conc.
- Low CO2 conc.
- High affinity of haemoglobin for oxygen
- Results in oxygen being associated.
Explain the affinity of haemoglobin for oxygen on respiring tissues.
- Low O2 conc.
- High CO2 conc.
- Low affinity of haemoglobin for oxygen
- Results in oxygen being dissociated.
Why do different haemoglobins have different affinities for oxygen?
The shape of the molecule.
- Each species produces haemoglobin with slightly diff amino acid sequence.
- Different tertiary and quaternary structures and so diff oxygen binding properties.
- Molecules range from those with high affinity for oxygen to those with low.
What happens when haemoglobin is exposed to different partial pressures of oxygen?
It does not bind to oxygen evenly.
The graph of this relationship is the oxygen dissociation curve.
What does the oxygen dissociation curve depict?
The relationship between the saturation of haemoglobin with oxygen and the partial pressure of oxygen.
Why is the gradient of the oxygen dissociation shallow initially?
- Shape of haemoglobin changed as each oxygen binds as they are closely united.
- At low oxygen concentrations, little oxygen binds to haemoglobin.
- The gradient of the curve is shallow initially.

What is the second stage of the oxygen dissociation curve?
- After first oxygen is bound
- quaternary structure of the haemoglobin changes.
- This change makes it easier for the other subunits to bind to an oxygen molecule.

Explain the third stage of the oxygen dissociation curve.
- After first and second oxygen is bound
- A smaller increase in the partial pressure to oxygen is needed to bind the second oxygen molecule
- Positive cooperativity because binding of the first molecule makes binding of the second easier and so on.
- The gradient of the curve steepens.

Explain the fourth and final stage of the oxygen dissociation curve
- Three oxygen bound and situation changes.
- Harder to attach last oxygen
- Due to probability.
- 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 gradient of the curve reduces and the graph flattens off.

At the gas exchange surface, why is the concentration of carbon dioxide low?
- It diffuses across the exchange surface and is excreted from the organism.
- Affinity of haemoglobin for oxygen is increased
- And high concentration of oxygen in the lungs
- oxygen is readily loaded by haemoglobin.
- This reduces CO2 concentration has shifted the oxygen dissociation curve to the left.

In rapidly respiring tissues why is the concentration of carbon dioxide high?
- The affinity of haemoglobin for oxygen is reduced
- low concentration of oxygen in the muscles
- oxygen is readily unloaded from the haemoglobin into the muscle cells.
- The increased CO2 concentration had shifted the oxygen dissociation curve to the right.

What does it mean if the oxygen dissociation curve is more to the left of the curve in its position on the axes?
The greater the affinity of haemoglobin for oxygen (It loads oxygen readily but unloads it less easily)
What does it mean if the oxygen dissociation curve is more to the right of the curve in its position on the axes?
The lower the affinity of haemoglobin for oxygen
So loads oxygen less readily but unloads it more easily.












