"Each haemoglobin molecule comprises two pairs of haem-globin molecules. In haemoglobin A (HbA), the predominant form in adults, the two polypeptide chains are termed the α chains and β chains, so haemoglobin A is styled α2β2. A small percentage (2.5%) of the normal haemoglobin in adults is haemoglobin A2 (HbA2), which contains δ chains instead of β chains, thus α2δ2."
"The affinity with which oxygen binds to the haemoglobin is modified by pH (Bohr effect 2), body temperature and the concentration within red cells of a molecule known as 2,3-bisphosphoglycerate (2,3-BPG), dependent, in turn, on the partial pressure of oxygen (pO2) 3,4."
"Following the release of oxygen in tissues, the sixth binding site of the iron atom (see above) becomes vacant, and the molecule is now known as deoxyhaemoglobin 5. In this state, each haemoglobin molecule has 4 unpaired electrons, rendering it paramagnetic. This change (from diamagnetic oxyhaemoglobin to paramagnetic deoxyhaemoglobin) is exploited in a number of MRI sequences (e.g. visualising veins on susceptibility-weighted imaging (SWI) and areas of brain activity on BOLD fMRI)"
"Carbon monoxide (CO) binds to haemoglobin forming carboxyhaemoglobin (COHb). Carbon monoxide has a stronger affinity than oxygen for haemoglobin, thus displacing the oxygen from the haemoglobin, such that less oxygen is available to the tissues."
Expected headings
"Structure"
"Physiology"
"Related pathology"
"The affinity with which oxygen binds to the haemoglobin is modified by pH (Bohr effect 2), body temperature and the concentration within red cells of a molecule known as 2,3-bisphosphoglycerate (2,3-BPG), dependent, in turn, on the partial pressure of oxygen (pO2) 3,4."
"Following the release of oxygen in tissues, the sixth binding site of the iron atom (see above) becomes vacant, and the molecule is now known as deoxyhaemoglobin 5. In this state, each haemoglobin molecule has 4 unpaired electrons, rendering it paramagnetic. This change (from diamagnetic oxyhaemoglobin to paramagnetic deoxyhaemoglobin) is exploited in a number of MRI sequences (e.g. visualising veins on susceptibility-weighted imaging (SWI) and areas of brain activity on BOLD fMRI)"