Mass transport in animals
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Haemoglobin
Large globular proteins with a quaternary structure ( four polypeptide chains : 2 alpha 2 beta)
Erythrocytes
Red blood cell
Adaptations of red blood cell
Bioconcave = Large SA Flat and thin ( Short diffusion distance to oxygen)
Where does oxygen bind to on the haemoglobin
The iron ion
Each chain contains..
A prosthetic haem group to bind to oxygen ( Can bind to 4 oxygen molecules in total and 8 atoms of oxygen as its diatomic )
What does oxygen binding to haemoglobin form
oxyhaemoglobin
Where does oxygen dissociate and associate from the haemoglobin
Oxygen associates with the haemoglobin at the lungs and dissociates with the haemoglobin at respiring tissues
Affinity for oxygen (Attraction of oxygen)
Partial pressure of oxygen Haemoglobin saturation Partial pressure of carbon dioxide
Partial pressure of oxygen
Measure of concentration of oxygen in a mixture of gases ( High in lungs, low in muscles)
Higher concentration of oxygen =
Higher oxygen = haemoglobin affinity increases
Saturation of haemoglobin
As haemoglobin binds to one oxygen molecule, it changes shape which makes it easier for more oxygen molecules to bind
The bohr effect
The effect of CO2 on the graph. more co2 shift to right and more acidic. less co2 shift to left lesa cidic
Why does co2 make the blood more acidic
CO2 reacts with H2O to form H+ ions
High co2 makes blood more acidic and lowers pH in the blood causing..
The haemoglobin molecules to associate less readily with oxygen and dissociate more readily. (Usually does this at respiring muscles where the concentraion of co2 is the greatest)
Low co2 makes blood less acidic and increases pH in the blood causing..
The haemoglobin to associate more readily with and oxygen and dissociate less readily ( Usually at the lungs so it can get the highest amount of co2 possible)