3.3.4.1 - Mass transport in animals Flashcards
How does the structure of red blood cells link to their function?
- biconcave disc - high SA:V ratio
- No nucleus or organelles - contains only haemoglobin which improves the oxygen carrying capacity
- Flexible - allows oxygen to pass through narrow capillaries
Describe the primary structure of haemoglobin
two alpha and two beta polypeptide chains
Describe the secondary structure of haemoglobin
each polypeptide chain is coiled into a helix
Hydrogen bonds
Describe the tertiary structure of haemoglobin
each polypeptide chain is folded into a precise shape
Hydrogen, ionic and disulphide bonds
Describe the quaternary structure of haemoglobin
- all four polypeptides are linked to form a spherical shape
- each polypeptide chain is associated with a haem group
How does the structure of haemoglobin help overcome the lack of solubility in oxygen?
- hydrophillic R groups face out, which maintains solubility
- this allows oxygen to be transported effectively once it binds to the iron containing haem group
Define affinity
attraction between molecules that results in the formation of a new molecule
Define partial pressure
measure of oxygen concentration in cells
Define association
process by which haemoglobin binds with oxygen
Define dissociation
process by which haemoglobin releases its oxygen
How does the affinity of haemoglobin change based on the environment?
- Site of gas exchange (alveoli) - high partial pressure of oxygen so haemoglobin has a **high oxygen affinity and readily associates **
- Site of respiration - low partial pressure of oxygen so haemoglobin has a low oxygen affinity and readily dissociates
What two factors affect the type of haemoglobin present in an organism?
- high altitude - increased affinity for oxygen (oxygen loads more readily as there is a limited supply)
- high metabolic rate - decreased affinity for oxygen (oxygen unloads more readily for respiration)
Describe the trend of an oxygen dissociation curve in humans?
- curve is initially shallow - at low partial pressure little oxygen binds to the haemoglobin (due to the shape it is difficult for the first molecule to bind)
- gradient on the curve** steepens** - once the first oxygen molecule has bound, the quaternary structure changes which changes the haemoglobin shape - this induces other subunit to bind
- (POSITIVE COOPERATIVITY) - it takes a smaller increase in partial pressure to bind the second oxygen
- graph plateaus - majority of binding sites are now occupied (3/4) so there is a** lower probability of an oxygen molecule bonding to an empty haem group**
What does a steep increase mean on an oxygen dissociation curve?
enables a large change in the haemoglobin saturation with a small change in oxygen partial pressure
What doe the Bohr shift show?
movement of the oxygen dissociation curve to the right due to increased carbon dioxide levels
(when the partial pressure of carbon dioxide is high, haemoglobins affinity for oxygen is reduced)
Describe the effects of increasing carbon dioxide on oxyhaemoglobin dissociation
- highly respiring tissues produce a lot of carbon dioxide
- this decreases the affinity of haemoglobin for oxygen (as there is a lower oxygen partial pressure)
- so there is increased unloading of oxygen at respiring tissues
Describe the Bohr shift in respiring tissues
- ** carbon dioxide concentration increases *and dissolves in the blood plasma
- carbon dioxide forms carbonic acid
- increase in the H+ ion concentration so pH of blood plasma decreases
- oxygen affinity of haemoglobin is reduced so oxygen is more readily dissociated *
- MORE oxygen is available for respiration at the same partial pressure
Describe the Bohr shift in gas exchange surfaces such as the alveoli
- Bohr effect is reversed
- concentration of carbon dioxide is lower
- haemoglobin has a higher affinity for oxygen (due to the increased pH)
- oxygen associates more readily
- more oxygen is taken in at the same partial pressure
How does the oxyhaemoglobin dissociation curve for a lugworm compare to a human?
- curve is** shifted to the left**
- lugworms live in burrows and when the tide goes out burrow contains progressively less oxygen (low partial pressure) - depleted oxygen environment
- difficult for oxygen association to occur
- so the lugworm haemoglobin has a HIGHER affinity for oxygen (so it if fully loaded even when there is minimal in the environment)
How does the oxyhaemoglobin curve of the Llama compare to a human?
- Curve is shifted to the left
- ** High altitude **so partial pressure of oxygen is low
- difficult for oxygen association to occur
- haemoglobin has a higher affinity for oxygen
How does the oxyhaemoglobin curve of a bird or small mammal compare to a human?
- curve is shifted to the right
- high metabolic rate - high oxygen demand
- so haemoglobin has a lower affinity for oxygen
- so oxygen dissociates more readily for use in respiration
Define saturation
when all the oxygen binding sites are taken up (so haemoglobin contains four oxygen molecules)
What two factors determine whether an organism will have a specialised transport system or pump?
They need a pump if…
1. high metabolic rate
2. small surface area to volume ratio - greater need for a pump as substances need to travel further
Why is it important that mammals have a closed, double circulatory system?
allows pressure to be increased and decreased depending on where in the body blood is going
** lungs - blood pressure is reduced** but if this passed to the rest of the body circulation would be very slow
* Heart - **pressure is increased **before being circulated to the rest of the tissues - allows substances to be delivered quickly which is important as mammals have a high temp and rate of metabolism