Mass Transport (haemoglobin)

Question 1

Binding one molecule of oxygen to haemoglobin makes it easier for second oxygen molecules to bind

Answer 1

Binding of first oxygen changes tertiary Structure of haemoglobin.
Leads to another binding site

Question 2

Explain how changes in shape of haemoglobin result in the S-shaped sigmoid Oxy haemoglobin dissociation curve

Answer 2

First oxygen binds to haemoglobin causing change in shape of binding site.
Shape change of haemoglobin allows more oxygen bind easily.

Question 3

Haemoglobin is a protein with a quaternary structure . Explain the meaning of quanternary struture.

Answer 3

Molecules contain more than one polypeptide chain.

Question 5

Describe the advantage of Bohr effect during intense exercise

Answer 5

Increase dissociation of oxygen.
For aerobic respiration at the cells.
Therefore anaerobic respiration delayed at the cells, less lactate at the cell

Question 6

Describe and explain the effect of increasing CO2 concentration on dissociation of Oxy haemoglobin

Answer 6

Increases oxygen unloading.
By decrease blood pH

Question 7

Why curve shifts left when diving

Answer 7

Higher affinity for oxygen than haemoglobin.
Allows aerobic respiration when diving at lower partial pressure of oxygen.
Therefore delay anaerobic respiration .

Question 8

Animals living at high altitudes shift to left.

Answer 8

High altitudes have low paprtial pressure of oxygen.
High affinity of haemoglobin with oxygen at low partial pressure of oxygen.
Sufficient oxygen supplied to respiring cells or tissues.

Question 9

Why small animals have curved to the right

Answer 9

Mouse haemoglobin has lower affinity for oxygen.
More oxygen can be unloaded for metabolic reaction.

Question 10

Why curve to the right for more active animals

Answer 10

Curve to the right so lower affinity of haemoglobin.
Haemoglobin unloads more readily.
More oxygen to cells.
For faster respiration .
That they have more faster metabolism.