Haemoglobin As

Question 1

how many polypeptides does haemoglobin have

Answer 1

4

Question 2

how many haem groups does haemoglobin have

Answer 2

4

Question 3

how many oxygen can each molecule of haemoglobin carry when fully saturated

Answer 3

4

Question 4

what type of molecule is haemaglobin

Answer 4

a protein

Question 5

where is haemoglobin found

Answer 5

red blood cells

Question 6

where does haemoglobin pick up oxygen

Answer 6

the lungs

Question 7

at a high or a low partial pressure does haemoglobin load oxygen

Answer 7

high

Question 8

where does haemoglobin unload the oxygen

Answer 8

respiring tissues

Question 9

what causes different types of haemoglobin

Answer 9

different primary structure

Question 10

does haemoglobin have a tertiary or quaternary structure

Answer 10

quaternary

Question 11

what chemical concentration is linked to unloading oxygen

Answer 11

high concentration of carbon dioxide

Question 12

why is there a sigmoid shaped dissociation curve

Answer 12

first oxygen binds to haemoglobin causing small change in shape
this makes it easier for more oxygen to bind

Question 13

what shape is a sigmoid curve

Answer 13

S shaped

Question 14

which way would the curve be shifted for an organism with a high metabolic rate

Answer 14

the right

Question 15

what does a curve shifted to the right mean for properties of the haemoglobin

Answer 15

lower affinity for oxygen
dissociates to respiring tissues more readily at higher partial pressure of oxygen
more oxygen for respiration more respiration for e.g. more heat

Question 16

what does a curve shifted to the left mean about properties of the haemoglobin

Answer 16

haemoglobin has a higher affinity for oxygen

haemoglobin saturated and dissociated at lower partial pressure of oxygen

Question 17

how would people with the same type of haemoglobin load more oxygen

Answer 17

have more red bloods cells so more haemoglobin

Question 18

how does changes in CO2 concentration affect the curve

Answer 18

more respiration
more CO2
lower pH
reduced affinity for oxygen by changing shape of haemoglobin
shifts curve right