haemaglobin

Question 1

describe the structure of haemoglobin

Answer 1

• a globular protein with a quaternary structure
• 4 polypeptide chains
• 4 haem groups each with an ion of iron
• 1 molecule binds to 4 oxygens as they each bind to a haem group

Question 2

give the adapations of red blood cells

Answer 2

• bi concave disc to increase surface area
• no nucleus which increases storage room for oxygen

Question 3

desribe what happens at the lungs

Answer 3

• there is a high partial pressure of oxygen at the lungs
• therefore more oxygen can bind to the haemoglobin and associate as the haemoglobin will have a higher affinity for oxygen
• this is also known as the loading of oxygen

Question 4

what happens at the respiring cells/tissue

Answer 4

• there is a low partial pressure of oxygen in the respiring cells
• therefore haemoglobin has a lower affinity for oxygen and it will dissociate
• this is also known as the unloading of oxygen

Question 5

what is the difference between fetal haemoglobin and adult haemoglobin

Answer 5

fetal blood has a higher affinity for oxygen and so this ensures that the fetus gets enough oxygen for development

the haemoglobin in the mothers blood has a lower affinity for oxygen which allows oxygen to dissociate and bind to the fetal haemoglobin

Question 6

explain the Bohr effect