Haemoglobin Flashcards

1
Q

What is the structure of haemoglobin?

A

2 alpha chains
2 beta chains
prosthetic group: haem - Fe2+

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
2
Q

What is the partial pressure of a gas?

A

pressure of a particular gas which contributes to the total pressure of gas mixture

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
3
Q

What is the relationship between pO2 and stauration of haemoglobin?

A

start: slow increase in saturation -> hard for first O2 to bind
rapid increase in saturation as easier for subsequent O2 to bind (cooperative binding)
slows down towards 100% as less likely O2 collide with unoccupied haem group

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
4
Q

What happens to haemoglobin when 1 O2 binds?

A

conformational change
haemgroups become more exposed

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
5
Q

Why doesn’t haemoglobin unload oxygen before reaching respiring tissue?

A

pO2 is not low in arteries due to thick wall

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
6
Q

What is the bohr effect?

A

fall in pH reduces the affinity of haemoglobin for oxygen causing increased unloading of O2 from haemoglobin

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
7
Q

Why does the bohr effect happen?

A

increased CO2 causes formation of carbonic acid which lowers pH

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
8
Q

Why is the bohr effect advantageous to metabolically active tissue?

A

rate of respiration increases and pCO2 increases causing rapid unloading
therefore plenty oxygen for aerobic respiration (less lactic acid produced)

How well did you know this?
1
Not at all
2
3
4
5
Perfectly