Oxygen transport Flashcards
oxygen systemic arterial partial pressure
between 75mmHg- 100mmHg, 14kPa
how is oxygen carried in the blood?
small volume dissolves in blood, other becomes bound to haemoglobin
what is haemoglobin?
protein of a molecular weight of 64,500
4 globin subunits, 2 alpha and 2 beta chains, each 16KDa
one haem structure in each chain that binds to oxygen
explain haem structure
four pyrrole rings held together by methane bridges
centre of the pyrrole rings is a bivalent iron ion, held together by two ionic and two covalent bonds
oxygen binds reversibly to the iron ion with no change in valency, so the reaction is called oxygenation and not oxidation
haemoglobin function
carries 4 oxygen molecules to form oxyhemoglobin
O2 carrying capacity definition
the maximum amount of oxygen that can be combined with Hb which is limited by the number of binding sites and whether they are available
2 measurements of bound oxygen
oxygen concentration as ml O2/100ml of blood
percentage saturation of maximal oxygen capacity
what process occurs during the binding of oxygen atoms
positive cooperativity
explain positive cooperativity
binding of each oxygen molecule to the tetramer facilitates the binding of the next molecule which results in a sigmoidal dissociation curve
- first oxygen difficult to bind
- once first binds, conformation change occurs bringing forward the pyrrole groups, makes it easier for the next 2 to bind
- last one more difficult, as smaller chance that it binds to an unoccupied binding site
what does the curve facilitate?
unloading of oxygen at tissues where partial pressure is low
loading at the lungs where partial pressure is high
curved S shape advantages
flat upper portion means that if PO2 falls slightly that loading is hardly affected
central steep part of the curve means that peripheral tissues can withdraw large amounts of oxygen for only a small drop in capillary partial pressure
oxhaemoglobin saturation definition
haemoglobin is said to be saturated with oxygen when all four binding sites are occupied
factors affecting oxygen binding to haemoglobin
- increase in H+
- increase in PCO2
- temperature
- increase in 2,3 diphosphoglycerate
explain the resulting shift of the curve
rightward shift
favour unloading the oxygen, with more oxygen unloaded at a given partial pressure of oxygen within the tissue capillary
what is a name for this + definition?
Bohr Effect
shifting to the right due to the collective effect of partial carbon dioxide pressure and decrease in pH
allosteric binding of carbon dioxide
increase in H+ ions, protonate various amino acid residues, such as histidine allowing them to form ion pairs that stabilise the deoxyhaemoglobin in the T state
bohR Right