Mass transport in animals Flashcards
How does haemoglobin have a quaternary structure
Each haemoglobin is made up of 4 polypeptide chains. Therefore it has a quaternary structure as it is made up of more than one polypeptide chain
Why can haemoglobin bind to 4 oxygen molecules
Each polypeptide contains a haem group containing Fe2+ which binds one oxygen molecule
So each haemoglobin molecule can bind 4 oxygen molecules
What is the equation that shows how oxygen and haemoglobin combine
Oxygen+ Haemoglobin —> oxyhaemoglobin
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What does partial pressure of oxygen mean
A measure of the concentration of oxygen present in tissues
What does Loading mean (or association)
When oxygen is taken up by haemoglobin
What does Unloading mean (or dissociation)
When oxygen is released or given up by haemoglobin
What does affinity mean
How well the oxygen is binded to the haemoglobin
What does percentage saturation mean
The amount of oxygen combined with the haemoglobin
What is the formula for percentage saturation
Oxygenated haemoglobin divided by the maximum saturation x 100
No. of binding sites occupied by O2 molecules over maximum number of binding sites x 100
What does oxyhaemoglobin mean
Haemoglobin bound to oxygen
What are the features of the loading of oxygen at the lungs
High partial pressure of oxygen
Haemoglobin has a high affinity for oxygen
Haemoglobin becomes saturated with oxygen
What are the features of the unloading of oxygen at the lungs
Low partial pressure of oxygen
Haemoglobin has a low affinity of oxygen
Haemoglobin becomes less saturated with oxygen
What shape is an oxygen dissociation curve always
S shape or Signoid
Why is the oxygen dissociation curve an S shape
This is because binding of the first molecule of oxygen to haemoglobin changes the tertiary structure and alters the structure of haemoglobin
This uncovers another haem group for oxygen to bind to
So oxygen molecules will bind more readily to the haemoglobin
Why is it good if the graph has flattened out
The haemoglobin will still stay fully saturated
Why is unloading useful on graphs
More oxygen is present so aerobic respiration occurs which means more ATP is produced so theres a higher uptake of oxygen. This prevents the onset of anaerobic respiration
What happens to the oxygen dissociation curve when in the presence of carbon
It will shift to the right
Because the affinity of haemoglobin for oxygen is reduced
So at the partial pressure of oxygen found at the tissues haemoglobin is less saturated
Oxygen unloads more readily to be used for aerobic respiration at the tissues
This delays the onset of anaerobic respiration at the tissues so less lactic acid is produced
Why is less lactic acid produced
CO2 lowers the pH of the blood alters the tertiary structure of haemoglobin
Why do organisms that possess haemoglobin not live in the same environment
As a result have very different amounts of oxygen available to them
Due to the way some organisms bodies work they may require their haemoglobin to be adapted to a higher or lower metabolism
What does metabolism mean
Rate of reactions in organisms cells
What have occurred which have resulted in their haemoglobin having differences in the position of dissociation curve
Mutations
What people would have a normal level of haemoglobin
Found in adult humans and many other species that live on land at sea level
What species have haemoglobin that is higher
Found in species that live in environments where the environmental partial pressure of oxygen is low
As there isnt a lot of O2 available in the environment normal haemoglobin would not fully saturate at the gas exchange surface
Instead they have a form of haemoglobin where the dissociation curve is shifted to the left
The haemoglobin will fully saturate at the lower environmental partial pressure of oxygen
Human foetal haemoglobin has a curve similar to this
What species have haemoglobin that is lower
This form of haemoglobin has a curve shifted to the right and is characteristic of species that have a high metabolic rate
The curve was much steeper and this means that the haemoglobin will unload its oxygen much faster as the red blood cells pass into the tissue
What happens when the oxygen dissociation curve shifts to the left
Haemoglobin has a higher affinity of oxygen
At the partial pressure of oxygen found at the gas exchange surface haemoglobin is more saturated with oxygen
So haemoglobin loads oxygen more readily and can be transported to tissues for aerobic respiration
Why must foetal haemoglobin have a curve to the left of adult haemoglobin
So that it has a higher affinity than its mothers haemoglobin
So oxygen loads onto foetal haemoglobin from the mothers haemoglobin
To be used for aerobic respiration
What happens when the oxygen dissociation curve shifts to the right
Haemoglobin has a lower affinity for oxygen
At the same partial pressure of oxygen found in tissues haemoglobin is less saturated with oxygen
So haemoglobin unloads oxygen more readily at tissues for faster aerobic respiration