Mass transport in animals Flashcards
where is it found
Red blood cells(erythrocytes)
structure of haemoglobin
It is a quaternary structured protein as it is made of 4 polypeptide chains . Each polypeptide chain contains a haem group containing iron ion which combines to oxygen.
How does haemoglobin load and unload oxygen
Haemoglobin can carry 4 oxygen molecules one at each haem group. In the lungs , at a high partial pressure haemoglobin has a high affinity for oxygen and as a result it readily associates with haemoglobin. At respiring tissues at a low partial pressure oxygen dissociates from haemoglobin because theres low affinity for oxygen
Bhor effect
As concentration of CO2 is high the rate of unloading is faster. This is advantageous as it provides more oxygen for respiring tissue that are undergoing aerobic respiration
importance of haemoglobin in movement in cells
Haemoglobin is required to load and unload oxygen. Also movement of CO2 is controlled by ventilation so it allows the Bohr effect to take place as there will always be a lower concentration of oxygen at respiring cells and higher concentration of CO2. As a result unloading oxygen is quicker to supply cell with oxygen. Oxygen is required for metabolic processes such as respiration to produce ATP from oxidative phosphorylation. This energy that is released from ATP is used for muscle contraction or for moving substances against concentration gradient such as sodium ions