mass transport in animals Flashcards
what is the role of haemoglobin and where is it found?
-it is found in red blood cells
-role is to carry oxygen around the body
-there are chemically similar types of haemoglobin found in other organisms, which carry out the same function
-it is found in earthworms, starfish, some insects, some plants and some bacteria
what is the structure of haemoglobin?
-large protein with a quaternary structure
-made up of four polypeptide chains
-each chain has a haem group which contains and iron ion and gives haemoglobin its red colour
-each molecule can carry four oxygen molecules
when is oxyhaemoglobin made?
in the lungs, when oxygen joins to haemoglobin during gas exchange
write the haemoglobin - oxyhaemoglobin reversible reaction.
associating/loading
Hb + 4O2 <–> HbO8 disassociating/ unloading
what does ‘affinity for oxygen mean’ and what is haemoglobins?
the tendency a molecule has to bind with oxygen.
haemoglobins affinity varies depending on the conditions its in, including the partial pressure of oxygen (pO2)
what does partial pressure of oxygen (pO2) mean?
a measure of oxygen concentration
the greater the concentration of dissolved oxygen in cells, the higher the partial pressure
relate partial pressure of oxygen to haemoglobin.
as pO2 increases, haemoglobins affinity for oxygen also increases.
-oxygen loads onto haemoglobin to form oxyhaemoglobin where there’s a high pO2
-oxyhaemoglobin unloads its oxygen where there’s a lower pO2
describe these 4 features at the alveoli and respiring tissues:
-oxygen concentration
-pO2
-affinity for oxygen
-loads or unloads
alveoli:
-HIGH oxygen concentration
-HIGH pO2
-HIGH affinity
-oxygen LOADS
respiring tissues:
-LOW oxygen concentration
-LOW pO2
-LOW affinity
-oxygen UNLOADS
what does an oxygen dissociation curve show?
how saturated the haemoglobin is with oxygen at any given partial pressure.
the affinity for haemoglobin for oxygen affects how saturated the haemoglobin is
what are the two axis on an oxygen dissociation curve?
Y= %saturation of haemoglobin with oxygen
X= partial pressure of O2 / kPa
why is an oxygen dissociation curve an ‘s’ shape?
because the saturation of haemoglobin can also affect the affinity
how does the saturation of haemoglobin affect its affinity?
-when haemoglobin binds with the first oxygen molecule, its shape alters in a way that makes it easier for the other O2 molecules to bind
-however as the haemoglobin gets too saturated, it gets harder for oxygen molecules to join
-this means the curve is a bit steeper in the middle where its easy for oxygen molecules to join and shallower bits at the start and end
how does the partial pressure of carbon dioxide (pCO2) affect oxygen unloading and how does this affect the dissociation curve?
-haemoglobin gives up more oxygen readily at a higher pCO2
-when cells respire they produce CO2 which raises the pCO2 causing more oxygen to be unloaded
-the dissociation curve ‘shifts’ to the right
-this is called the Bohr effect
what type of haemoglobin do organisms in low oxygen environments (e.g. lugworms) have and how does this effect the dissociation curve?
-haemoglobin with a higher affinity for oxygen
-this is because there is less oxygen available, so the haemoglobin needs to be good at loading any available
-the dissociation curve is to the left of ours
what type of haemoglobin do organisms in high activity level (e.g. birds) environments have and how does this effect the dissociation curve?
-has a lower affinity for oxygen
-their haemoglobin needs to be able to unload oxygen easily so its available for them to use
-the dissociation curve sits to the right of humans