Haemoglobin Erythrocytes are RBCs Adaptations: Biconcave shape maximises surface area for gas exchange Small and

flexible to pass through narrow capillaries No nucleus- more room to carry gases Packed with haemoglobin

Haemoglobin Haemoglobin made up of 4 globular proteins and 4 iron ions (haem) It has an affinity for oxygen (likes to hold onto it)- can carry 4 oxygen molecules Quaternary structure of 4 polypeptide chains

In the lungs: Lungs have high partial pressure So oxygen diffuses into blood plasma then down concentration gradient into RBCs. Oxygen binds to haem of haemoglobin (associates) Oxygen and haemoglobin = oxyhaemoglobin

In muscles: Oxygen used for respiration so lower partial pressure Oxygen diffuses from RBC to muscle tissue down concentration gradient Haeomoglobin dissociates (oxygen leaves)

Partial Pressure o o o Oxygen concentration = partial pressure (kPa) Ventilation allows lung tissue to have high partial pressure Percentage of saturated haemoglobin highest here

Higher the partial pressure, the higher the affinity Oxygen Dissociation Curve Very difficult to achieve 100% saturation As first oxygen molecule associates, conformation of haemoglobin changes o Makes it easier for 2nd and 3rd oxygens to associate o Since haemoglobin fuller, harder for 4th to associate o This is why curve plateaus

Further to the left the curve, higher the affinity

Foetal Haemoglobin In pregnancy, foetal and maternal blood kept separate To get oxygen from maternal blood to foetal blood, foetal haemoglobin need a higher affinity that maternal haemoglobin Stronger affinity means they can become saturated at a lower partial pressure

Carbon dioxide Carbon dioxide travels through blood either by: Diffuses into blood plasma Associates with haemoglobin to form carbahaemoglobin Transported as hydrogencarbonate ions

Some carbon dioxide from respiring cells diffuses into RBC and converted to carbonic acid This releases H+ protons and hydrogen carbonate ions- decreasing pH Hydrogen carbonate ions diffuse out of the RBC thus changing charge Therefore to balance charge, Cl- diffuses into cell (Chloride Shift) H+ ions can bind with haemoglobin to form haeomoglobinic acid. This changes the pH of the haemoglobin

In respiring tissue: More CO2 produced More carbonic acid formed More H+ disassociated More competition for Hb More oxygen disassociation

Carbon dioxide reduces affinity of oxygen Bohr Effect: The more carbon dioxide, the lower oxygen affinity (more it disassociates) so curve shifts to right. Organisms living with low concentrations of oxygen tend to have high oxygen affinities Active organisms have high oxygen demands so have lower oxygen affinities so the oxygen can be shared quickly to the respiring cells. Increase in carbon dioxide, reduces pH, lower affinity