3B Mass Transport Flashcards
What kind of protein is haemoglobin?
- globular
What is haemoglobin?
- an oxygen-carrying pigment found in vast quantities in red blood cells
Describe the structure of red blood cells
- biconcave discs for high SA:V ratio
- no nucleus
- more space for haemoglobin for more oxygen transport
Describe the quaternary structure of haemoglobin
- made up of 4 polypeptide chains (globin proteins)
- made of 2 alpha globins and 2 beta globins
- each globin has a prosthetic haem group
How are the 4 globin subunits held together and arranged in haemoglobin?
- held together by disulphide bonds
- arranged with hydrophobic R groups facing inwards which preserves the 3D spherical shape
Why does the hydrophilic R groups facing outwards in haemoglobin benefit the molecule?
- it maintains solubility
Why is the arrangement of the R groups within haemoglobin important for its function?
- if changes occur to amino acid sequence, the function of the protein can change
- eg. in sickle cell anaemia, valine (non-polar) replaces glutamic acid (polar) which affects solubility of haemoglobin (lessens it)
Describe the importance of the prosthetic haem groups in haemoglobin
- prosthetic haem group contains an iron (II) ion (Fe2+) which is able to reversibly combine with an oxygen molecule
- this forms oxyhaemoglobin
- the presence if this causes blood to appear bright red in colour
How many oxygen molecules can each haemoglobin molecule carry?
- 4
- each haem group can carry one molecule
Are all haemoglobin molecules the same?
- the haem group is the same for all types of haemoglobin
- the globin chains can differ lots from different species of haemoglobins
Describe the function of haemoglobin
- responsible for binding oxygen in the lung and transporting oxygen to the tissue to be used in aerobic metabolic pathways (respiration)
How does haemoglobin help with transport of oxygen?
- oxygen isn’t very soluble in water
- haemoglobin is soluble in water
- oxygen can be carried more efficiently around the body when bound to haemoglobin
What does the presence of the haem group enable?
- enables small molecules like oxygen to be bound more easily because as each oxygen binds the quaternary structure is altered
- this is due to changes in the teriary structure
- this causes haemoglobin to have a higher affinity for subsequent oxygen molecules
Describe cooperative binding of haemoglobin
- binding of first oxygen molecule results in a conformational change in the structure of the haemoglobin molecule
- this makes it easier for each successive oxygen molecule to bind
What does the existence of the iron (II) ion in the prosthetic haem group allow?
- allows oxygen to reversibly bind to form oxyhaemoglobin
Which oxygen is hardest to dissociate from the haemoglobin?
- the last one
Describe what partial pressure is
- the pressure of the gas if the gas were in the same volume and temperature by itself
- it can change with altitude
Does altitude affect % composition of a mixture of gases?
no
What does the oxygen dissociation curve describe?
- the relationship between the partial pressure of oxygen and the % saturation of haemoglobin with oxygen
Why can haemoglobin pick up lots of oxygen in the lungs?
- low CO2 in lungs so haemoglobin can pick up more oxygen
- also a high partial pressure of oxygen in the lungs
Why is oxygen dropped off by haemoglobin in respiring tissues?
- the partial pressure of oxygen is low
- the oxygen diffuses out into the body cells down a conc grad
Why can a small change in partial pressure of oxygen have a very large effect on the % saturation of haemoglobin with oxygen?
- because haemoglobin has such a high affinity for oxygen
How does the partial pressure of oxygen in different areas of the body help with transport of oxygen?
- it ensures oxygen is picked up from where there is lots of it and dropped off to where there is less of it
How does pH alter haemoglobin?
- CO2 makes blood more acidic
- pH alters the hydrogen bonds in haemoglobin
What does the Bohr shift explain and how?
- explains how the ability of haemoglobin to bind to and release oxygen changes
- when partial pressure of CO2 is high (eg. in respiring tissues) haemoglobin’s affinity for oxygen is reduced
- this is because CO2 lowers the pH of the blood by forming carbonic acid and causes the release of oxygen
- CO2 in the lungs is comparatively lower so haemoglobin’s affinity for oxygen is increased
- causes easier binding
How does more CO2 affect the position of the oxygen dissociation curve?
- more CO2 shifts the dissociation curve to the right
What can have a major impact on the evolution of haemoglobin within a species?
- environmental factors
Describe the effects of altitude on haemoglobin
- the pp of oxygen is lower at higher altitudes
- species living at high altitudes have haemoglobin that is adapted to these conditions
- eg. llamas have haemoglobin that binds much more readily with oxygen
- this is beneficial as it allows them to obtain a sufficient level of oxygen saturation in their blood when the pp of oxygen is low
Describe the deer mouse’s haemoglobin
- they populate much of the US at high and low altitudes
- this species inhabits the widest range of altitudes of any north american mammal and it has a large degree of genetic variation for haemoglobin
Describe the lugworm and how its oxygen dissociation curve compares to that of a deer mouse
- lugworms live in low oxygen conditions
- luworm/high altitude deer mouse curve is to the right of the low altitude deer mouse’s curve and reaches 100% saturation quicker
Describe the adaptations of foetal haemoglobin
- more efficient at absorbing oxygen at lower concs
- vital as it allows for a baby to obtain oxygen from its mother’s blood (via placenta)
- oxygen conc in mother’s blood is lower than oxygen conc in the lungs
- after birth, the baby produces adult haemoglobin as it is more suited for uptake of oxygen from the air
Describe myoglobin and its adaptations
- ‘muscle haemoglobin’
- higher affinity for oxygen than foetal and adult haemoglobin
- myoglobin can take oxygen from adult haemoglobin
- used for storing oxygen in muscles
Compare the oxygen dissociation curves of myoglobin, foetal haemoglobin and adult haemoglobin
- myoglobin is furthest left
- foetal haemoglobin is in the middle
- adult haemoglobin is furthest right
What tends to be the case in larger more complex organisms in terms of their important exchange sites?
- they tend to be far away from other cells within the organism
Why is diffusion a non-viable method for transport of substances in larger organisms?
- the distance is too far and the process would be inefficient
- diffusion wouldn’t be fast enough for metabolic requirements of cells
- diffusion is only involved at exchange sites right at the start and end of the process
What is mass transport?
- the bulk movement of gases or liquids in one direction
- usually via a system of vessels and tubes
Describe generally the mammal circulatory system as a mass transport system
- one-way flow of blood carries nutrients and gases to all the cells of the body
What do mass transport systems help to do?
- help to bring substances quickly from one exchange site to another
- they also help maintain diffusion gradients at exchange sites and between cells and their fluid surroundings
- they ensure effective cell activity by keeping the immediate fluid environment of cells within a suitable metabolic range
Describe blood circulation within mammals (big and small)
- small animals with large SA:V can rely on diffusion to exchange oxygen, CO2 and nutrients
- larger animals have a smaller SA:V so diffusion alone is insufficient for exchange of materials
What do all organisms need to do?
Exchange materials with their environments
What are circulatory systems generally?
- systems which carry around fluids containing materials needed by the organism as well as waste that needs removing
Describe a closed circulatory system
- blood is pumped around the body and is always contained within a network of blood vessels
- possessed by all vertebrates and many invertebrates
Describe an open circulatory system
- blood isn’t contained within blood vessels but is pumped directly into body cavities
- possessed by arthropods and molluscs