3.4.1 Mass Transport in Animals Flashcards
Exchange and Transport
Haemoglobin
Large protein with quaternary structure, made of four polypeptide chains. Each chain has a haem group with an iron ion. Each haemoglobin can carry four oxygen molecules
Association/loading
Oxygen molecule joins to haemoglobin
Dissociation/unloading
Oxygen leaves oxyhaemoglobin
High partial pressure of oxygen
Haemoglobin affinity for oxygen increases. Oxygen loads onto haemoglobin to form oxyhaemoglobin where there’s a high pO2. Oxyhaemoglobin unloads its oxygen where there’s a lower pO2 (respiring tissues)
Dissociation curve
Binding of first O2 molecule alters shape and makes it easier for other O2 molecules to join. As haemoglobin becomes saturated, harder for other molecules to join
Carbon dioxide concentration
High CO2 concentration at respiring cells increases rate of oxygen unloading
Bohr effect
Saturation of blood with oxygen lower, so more oxygen being released. Dissociation curve shifts due to pCO2
Low oxygen environments
Organisms have haemoglobin with higher affinity for oxygen, good at loading oxygen
High activity levels
Haemoglobin with lower affinity for oxygen, need to easily unload oxygen at respiring tissue
Effects of size on haemoglobin
Small mammals have a higher surface area to volume ration, so high metabolic rate so high oxygen demand
Function of circulatory system
Multicellular organisms have low surface area to volume ration, require specialised mass transport system to carry raw materials from specialised exchange organs to cells
Pulmonary artery
Carries blood from the heart to the lungs
Pulmonary vein
Carries blood from lungs to the heart
Aorta
Carries blood from the heart to the body
Vena cava
Carries blood from the body to the heart
Renal artery
Carries blood from the body to the kidneys
Renal vein
Carries blood from the kidneys to the vena cava
Coronary arteries
The heart’s own blood supply, has a right and left one