Topic 3 - Structure of Haemoglobin & Oxyhaemoglobin Dissociation [7]

Question 1

Affinity

Answer 1

ability of haemoglobin to attract oxygen

Question 2

What is Myoglobin

Answer 2

a type of Haemoglobin that can hold oxygen at very low partial pressures

Question 3

Structure of Haemoglobin

Answer 3

4 Polypeptide chains, each chain containing a haem group. Haem groups have an iron in them and it carries an oxygen.

Question 4

Function of a Red blood cell?

Answer 4

Contain Haemoglobin so it can transport oxygen in the blood

Question 5

Unloading/dissociation of haemoglobin

Answer 5

unbinding/detaching of oxygen from haemoglobin

Question 6

Loading/association of haemoglobin

Answer 6

binding of oxygen to haemoglobin

Question 7

Saturation

Answer 7

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

Question 8

What is the Bohr Effect

Answer 8

when a high co2 conc causes the oxyhaemoglobin curve to shift to the right.
when theres lots of CO2 present, it will dissolve in blood and become acidic. changing shape of haemoglobin slightly.

Question 9

why is the oxyhaemoglobin dissociation curve said to have a “Cooperative Nature”

Answer 9

refers to how it is very hard for the first oxygen to bind but when it does, the haemoglobin changes shape and this makes it easier for the rest of the oxygens to bind

Question 10

what does the oxyhaemoglobin dissociation curve demonstrate

Answer 10

at high partial pressures, high affinity. (lots available, will load it up) haemoglobin will be almost completely saturated w oxygen
at lower partial pressures, there is a lower affinity. will actually unload in these regions.

Question 11

Describe the shape of Oxyhaemoglobin Dissociation Curve

Answer 11

Slight S shape curve / “sigmoid curve”