mass transport in animals

Question 1

affinity of haemoglobin for oxygen

Answer 1

the ability of haemoglobin to attract or bind oxygen

Question 2

saturation of haemoglobin with oxygen

Answer 2

when haemoglobin is holding the maximum amount of oxygen it can bind

Question 3

loading/ association of haemoglobin

Answer 3

the binding of oxygen to haemoglobin
take place in lungs

Question 4

unloading/ dissociation of haemoglobin

Answer 4

when oxygen detaches or unbinds from haemogloin

Question 5

what is haemoglobin and what is its role of in the transport of oxygen

Answer 5

-protein with a quaternary structure found in red blood cells

-binds to oxygen and carries it in the blood from the lungs to the rest of the body

Question 6

describe the structure of haemoglobin

Answer 6

-Quaternary structure

-made of 4 polypeptide chains ( 4 globular submits)

• globular submits: held together by disulphide bonds and arranged so that there hydrophobic r groups are facing inwards ( helps preserve the 3d spherical shape)
  and the hydrophilic r groups are facing outwards ( helps maintain solubility)

-each polypeptide chain contains a Haem group containing an iron ion ( Fe2+)which combines with oxygen
forms oxyhaemoglobin

red blood cells are biconcave Shape: Increases SA for rapid diffusion of O2
no nucleus : provides more space for haemoglobin to transport O2

Question 7

describe the functions of haemoglobin

Answer 7

1) responsible for binding O2 in lungs and transporting O2 to the tissues to be used in aerobic metabolic pathways

2) as O2 is not very soluble in water and haemoglobin is , oxygen can be carried more efficiently around the body when bound to haemoglobin

3) existence of iron ion in the haem group allows O2 to be reversibly bind