mass transport (exchange Flashcards
(123 cards)
what is the structure of haemoglobin
quaternary structure protein with 4 polypeptide chains , 2 alpha , 2 beta with each polypeptide chain associated with a haem group and a iron ion
how many oxygens can bind to one iron ion
1 oxygen molecule binds to one iron ion . therefore 4 o2 molecules can be carried by a single haemoglobin
what is the primary structure of haemoglobin
sequence of amino acids in the four polypeptide chains
what is the secondary structure of haemoglobin
each of these polypeptide chains is coiled into a helix
what is the tertiary structure of haemoglobin
each polypeptide chain is folded into a precise shape - an important factor in its ability to carry oxygen
what is the quaternary structure of haemoglobin
all 4 polypeptide chains are linked together to form an almost spherical molecule
when does haemoglobin dissociate and accociate with oxygen
haemoglobin associates with oxygen in the lungs and it dissociates in the tissues
what is the role of haemoglobin
to transport oxygen .
readily associate with oxygen at the surface where gas exchange takes place
readily dissociate from oxygen at those tissues requiring it
what is partial pressure of oxygen
p02 is a measure of oxygen concentration of dissoloved oxygen in cells
where is there a high p02
oxygen loads
where is there a low p02
oxygen unloads
will there be a high or low concentration of co2 in alveoli
low concentration
will there be a high or low concentration of co2 in the respiring tissue
high concentration
how does haeomoglobin change its affinity for oxygen
haemoglobin changes its affinity for oxygen under different conditions . it acheives this because its shape changes in the prescence of certain substances eg carbon dioxide
describe the quaternary structure of haemoglobin
four polypeptide chains joined 2 beta and 2 alpha . which link to form a spherical molecle each one with a haem group and fe2+ ion , meaning 4 o2 molecules can join to one haemoglobin
in the oxygen dissociation curve why is the partial pressure of oxygen low at the start
At the start there is a low po2 , haemoglobin had a high affinity for oxygen so there’s a low saturation , the shape of haemoglobin makes it difficult for the first oxygen molecule to bind , because the polypeptide subunits are closely United . This is in the respiring tissues ,
First oxygen binding causes a change in the quaternary structure which makes it easier for the other subunits to bind to an oxygen molecule . .
The curve shows positive cooperativista as it takes a smaller increase in the partial pressure of oxygen to bind to the second
Lastly it is difficult for o2 to load so slows down the rate , this is because high po2 , haemoglobin had a high affinity for o2 so there’s s high saturation . More binding sites occupied so gradient reduces and curve flattens off
What is partial pressure measured in
Kilopascals
What happens to the curve when co2 is higher
Shifts right
What happens when co2 is lower
Shifts left
Why does it shift right in prescence of co2
Ph decreases , tertiary structure changes and it unloads more . Never fully saturated , affinity for o2 is lower .
Why does it shift left with lower co2
Ph raised , less co2 , saturation of haemoglobin is higher , affinity is higher , it is loading more
What’s the shift called
The Bohr shift
What happens to the curve for the lugworm ( low o2 environment )
Shifts to the left , higher affinity for oxygen so has to load more and at a low partial prsssure of oxygen oxygen binds to haemoglobin very quickly . Another way is that it’s respiring less so less co2 is produced and needs to load more
What effect do hawks have on the curve ( they have a high respiratory rate)
More respiration , unloads at low partial pressures of oxygen there’s is a lot of co2 produced so shifts to the right