7-Mass Transport Flashcards
Haemoglobin Structure
PRIMARY- Sequence of amino acids in 4 polypeptide chains.
SECONDARY- Each polypeptide chain is coiled into a helix.
TERTIARY- Each chain is folded into a specific shape with the important ability to carry O2.
QUATERNARY- All 4 polypeptide chains are linked together to form an almost spherical shape. Each chain is attached to a haem group, containing a ferrous (Fe2+) ion. Each ferrous ion can bind to an O2 molecule so 4 O2 molecules can be carried by 1 haemoglobin molecule.
Loading (Associating)
Process of O2 binding with haemoglobin.
Unloading (Dissociation)
Process of haemoglobin releasing the attached O2.
Affinity of O2 in Haemoglobin
The likelihood for haemoglobin to take up O2. Haemoglobin with high affinity takes up O2 easier but releases it less easily and vice versa.
Haemoglobin’s Efficiency when Transporting O2
Readily associates with O2at surface where gas exchange takes place.
Readily dissociates with O2 at tissues requiring it.
Oxygen Dissociation Curve
1) At low O2 conc, less O2 binds with haemoglobin due to shape of haemoglobin molecule. This gives curve an initial shallow gradient.
2) The binding of the first O2 molecule induces the other subunits to bind to O2 because it changes its quaternary shape.
3) Positive Cooperativity occurs because binding of first molecule makes binding of second easier. Gradient of curve steepens.
4) After binding to 3rd molecule the 4th isn’t easier as it should be since it’s less probable for it to come in contact with O2. Gradient of curve reduces and curve flattens off.
Positive Cooperativity
A smaller increase in partial pressure of O2 is required for second molecule of O2 to bind to haemoglobin than first because it’s easier.
The further the Oxygen Dissociation Curve is to the left…
…The greater the affinity of haemoglobin for O2.
The further the Oxygen Dissociation Curve is to the right…
…The lower the affinity of haemoglobin for O2.
Effects of CO2 conc on Oxygen Dissociation Curve
At gas exchange surface there’s low CO2 conc so O2 affinity of haemoglobin is increased so O2 is loaded and curve shifts left.
At rapidly respiring tissues there’s high CO2 conc so O2 affinity of haemoglobin is decreased so O2 is unloaded and curve shifts right.
Loading, Transport & Unloading of Oxygen
1) CO2 constantly removed at gas exchange surface.
2) pH raised due to low CO2 conc which changes shape of haemoglobin into one that readily loads O2.
3) New shape also raises affinity of O2 for haemoglobin so O2 isn’t released when being transported in blood to tissues.
4) CO2 is produced by respiring cells in the tissues which lowers pH of blood.
5) Lower pH changes shape of haemoglobin to one with lower affinity of O2 so is released into respiring tissues.
Oxygen Dissociation Curve of a Lugworm
Shifted very far left than that of a human curve because it needs as much O2 as possible since it doesn’t move very far away from its burrow.
Closed Double Circulatory System of Mammals
Blood is confined to vessels and passes 2x through the heart for each complete circuit of the body.
Atrium
Thin walled and elastic and stretches as it collects blood.
Ventricle
Thick muscular wall since it has to contract strongly to pump blood, either to lungs or rest of the body.
Valves
Formation that prevents back flow of blood.
Aorta
Connected to left ventricle and carries deoxygenated blood from the heart to the rest of the body (except the lungs).
Vena Cava
Connected to right atrium and brings back deoxygenated blood from rest of the body (tissues).
Pulmonary Artery
Connected to right ventricle and carries deoxygenated blood to lungs where it’s O2 is replenished and CO2 is removed.
Pulmonary Vein
Connected to left atrium and brings oxygenated blood back from lungs.