Carbon monoxide poisoning is fatal. Carbon monoxide binds to haemoglobin at the same site as oxygen – the iron atom within the haem group – however carbon monoxide will bind with a strength 200 times that of oxygen. This means that if carbon monoxide is inhaled it was always displace oxygen within haemoglobin. If oxygen can no longer bind to haemoglobin then the respiring cells of the body can no longer receive oxygen and will eventually die. When carbon monoxide binds to haemoglobin it causes the haemoglobin to shift from the T form to the R form, so oxygen quickly binds to the other available haem groups within the haemoglobin. If carbon monoxide is only bound at one of the four haem sites within the molecule it can increase the affinity
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Currently there are over 1000 mutations know to have occurred to produce mutant haemoglobin molecules and over 90% of these mutant haemoglobins are caused by a single amino acid substitution caused by a point mutation in the DNA. (Voet and Voet) One example of a mutated haemoglobin is haemoglobin Helsinki. This is a very rare form of haemoglobin that occurs when lysine (a basic amino acid) is replaced with methionine (a non-polar amino acid) in the 82nd position in the beta globin chain. This substitution can cause reduced binging of BPG to deoxyhaemoglobin, so the haemoglobin is less likely to release oxygen into the tissues. Some of the clinical consequences of this include weakness, headaches, dizziness and lethargy as well as itching, bruising and abdominal pain. …show more content…
HbC results from a mutation that causes glutamine (an acidic amino acid) to be swapped for lysine (a basic amino acid) in the 6th position on the beta globin chain. This substitution can cause cellular crystallisation of oxyhaemoglobin, resulting in increased fragility. Whilst there are very few serious clinical consequences individuals with HbC have increased blood viscosity and their erythrocytes are more rigid and have a reduced survival time. On a rare occasion mild haemolytic anaemia and occasionally enlarged spleen may occur, although spleen function remains normal. (Baynes and
Currently there are over 1000 mutations know to have occurred to produce mutant haemoglobin molecules and over 90% of these mutant haemoglobins are caused by a single amino acid substitution caused by a point mutation in the DNA. (Voet and Voet) One example of a mutated haemoglobin is haemoglobin Helsinki. This is a very rare form of haemoglobin that occurs when lysine (a basic amino acid) is replaced with methionine (a non-polar amino acid) in the 82nd position in the beta globin chain. This substitution can cause reduced binging of BPG to deoxyhaemoglobin, so the haemoglobin is less likely to release oxygen into the tissues. Some of the clinical consequences of this include weakness, headaches, dizziness and lethargy as well as itching, bruising and abdominal pain. …show more content…
HbC results from a mutation that causes glutamine (an acidic amino acid) to be swapped for lysine (a basic amino acid) in the 6th position on the beta globin chain. This substitution can cause cellular crystallisation of oxyhaemoglobin, resulting in increased fragility. Whilst there are very few serious clinical consequences individuals with HbC have increased blood viscosity and their erythrocytes are more rigid and have a reduced survival time. On a rare occasion mild haemolytic anaemia and occasionally enlarged spleen may occur, although spleen function remains normal. (Baynes and