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Notes on gas exchange and mass transport
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Haemoglobin -transport oxygen
.
↑ polypeptides each associated wha haem
group (Felt)
"
·
structure :
,
↓ Felt can combine with
each an 02 molecule => 402 altogether
·
loading /associating :
haemoglobin binding to Q
·
unloading/dissociating :
haemoglobin releases O2
·
higher affinity of O2 = take up Of more easily but release it less easily
affinity for O2 under different conditions
·
Haemoglobin changes its
by changing shape
L Co present =
haemoglobin lower affinity to On , so releases O2
·
Different haemoglobin = different affinities for O2
>
-
Diff .
3/0 structure so diff -
binding properties
, Transport of Oz by haemoglobin
·
oxygen dissociation curve
ja
pOz
① shape of haemoglobin makes it difficult for the 1st O2 to bind to
haem group bc the polypeptides are so close together
>
-
little O2 binds - shallow curve initially
② Ist binding causes haemoglobin to change shape making , it
easier for other polypeptides to bind to O2 molecule
>
-
smaller increase in partial pressure of O2 to bind to 2nd O2 than
the 1st = the cooperativity
③ When haemoglobin tries to bond to the 4th O2 , most of the
binding sites have been occupied so less likely 7th O2 will find an
empty binding site
>
-
graph plateaus
·
Bohr Effect -
effect of [CO2] on oxygen affinity
-
Further to the left=greater affinity for O2
>
- loads O readily but unloads less easily
,
-
Further to the right lower affinity fo
=
O2
>
-
loadsOn less readily but unloads more easily
,
-greater conc .
of CO2 =
haemoglobin releases O2 more
readily
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