haemoglobin

Question 1

structure of haemoglobin

Answer 1

protein. has 4 polypeptides each associated with a haem group
each carry an oxygen molecule
different animals have different types of haemoglobin as they have different order of amino acids

Question 2

how does haemoglobin transport oxygen

Answer 2

haemoglobin carries oxygen and has a high affinity for it meaning it can form oxyhaemoglobin
resides in red blood cells
loading happened in the lungs
at high pp of o2
unloads/dissociates to respiring tissue
at low pp of o2
unloading also linked to higher carbon dioxide concentration

Question 3

why is the dissociation curve an s shape

Answer 3

first oxygen binds to haemoglobin causing change in shape. shape change allows more O2 to bind easily leading to a greater saturation with O2

Question 4

why are dissociation curves shifted to the right

Answer 4

haemoglobin has a lower affinity for oxygen
dissociates to respiring tissues more readily at higher partial pressure of oxygen
more oxygen to cells for more respiration to generate heat

in environment with lots of oxygen usually smaller animals with large sa to volume ratio and high respiration activity

Question 5

why are oxygen dissociation curves shifted to the left

Answer 5

haemoglobin has a higher affinity for oxygen

haemoglobin saturated and dissociates at a lower partial pressure of oxygen

Question 6

what is the effect of people having more red blood cells

Answer 6

have more haemoglobin so can load more oxygen. usually live in places with not very much oxygen

Question 7

what is the effect of having more respiration

Answer 7

more co2, lower pH, reduces affinity for oxygen by changing shape of haemoglobin shifts curve to the right