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how bpg acts as a haemoglobin regulator?
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BPG also known as 2,3 diphosphoglyceratye binds to
haemoglobin by lowering the o2 affinity of haemoglobin.
in the absence of BPG the p50 of haemoglobin is 1 torr in
its presence p50 becomes 26 torrs.
BPG lowers the o2 affinity of haemoglobin by a factor of 26
which is estimated in enabling haemoglobin to unload o2 in
tissue capillaries.
BPG reduces the o2 affinity of hb by binding in the
central cavity of deoxy haemoglobin and not to oxygenated form.
| Is This Answer Correct ? | 8 Yes | 2 No |
Answer / mark
2',3 BPG binds to haemoglobin when the HB is in its T
state. This interaction stabilises the T state cuasing a
lower affinity for oxygen. This means that oxygen is more
liklely to be delivered to the tissues when BPG is bound to
HB. A person at high altitude has a high concentration of
BPG in there blood for this reason. This would mean a lower
amount of oxygen in the air would still enable the same
amount of O2 to be delivered to the tissue (which of course
has limits, meaning that eventually the o2 level could be
so low that it is not being delivered to the tissues)
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