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how is oxygen carried in the blood
oxygen exchange at alveoli
oxygen transport
oxygen exchange at cells
carbon dioxide exchange at cells
carbon dioxide transport
carbon dioxide exchange at alveoli
reversible oxyhaemoglobin equation
haemoglobin + oxygen -- Oxyhaemoglbin
Hb + 4o2 --- HbO8
partial pressure
measure of the amount of a gas present in a mixture of gases
where is pO2 highest and lowest in the body
alveoli
body tissues after being used
describe the structure of haemoglobin
has 4 haem groups- they have an affinity for oxygen
is a globular protein
complex protein consisting of 4 subunits of 2 alpha chains and 2 beta chains
these each contain a central haem group containing Fe 2+
oxygen binds to the iron within the haem group

describe and explain the shape of the graph
sigmodial ( s-shaped) curve results from co-operative binding
at low pO2 it is difficult for hb to pick up O2
when one O2 binds to Hb, it distorts the shape of the molecule, making it easier for more o2 to bind
after 3 o2 have bound to hb, it is very difficult for the 4th to bind. even at high po2, it is difficult for hb to be fully saturated with o2

explain why the curve is different for foetal haemoglobin
foetal hb has a higher oxygen affinity than adult hb
because foetal hb needs to be able to pick up oxygen from the mothers blood in the placenta
which direction is the bohr shift
to the right
why is haemoglobin efficent at transporting oxygen
it can readily associate with oxygen at gas exchange surfaces
this will increase po2 in blood
why is haemoglobin again efficient at transporting oxygen
readily dissociate with oxygen ar the tissues
this will increase po2 in the tissues and decrease it in the blood
when does hb change its affinity for oxygen
under different conditions eg
low ph
high co2
what does the presence of co2 have on hb
makes hb associate less readily with o2
therefore releasing o2 in the presence of high co2 such as tissue
this is the bohr effect