Haemoglobin Flashcards

1
Q

What is haemoglobin?

A

A large protein with a quaternary structure: it is 4 polypeptide chains and 4 iron ion prosthetic groups which travels in blood to carry oxygen

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

Structure of haemoglobin

A

4 polypeptide chains
2 alpha glob in 2 beta globin
4 iron haem groups

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

Where does oxygen bind to in haemoglobin?

A

4 iron prosthetic groups

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

Loading and unloading of oxygen to haemoglobin

A

Haemoglobin + 4 oxygen to form oxy haemoglobin
A reversible reaction so oxy haemoglobin can unload all 4 oxygen

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

Loading

A

Oxygen binds to iron in haemoglobin

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

Unloading

A

Oxygen unbinds from oxyhaemoglobin

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

What does the loading of oxygen onto haemoglobin depend upon?

A

The affinity haemoglobin has for oxygen

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

What affects the affinity haemoglobin has to oxygen?

A

The partial pressure of oxygen in the area

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
9
Q

Trend for oxygen loading onto haemoglobin

A

Where there is a high partial pressure for oxygen, oxygen will unload onto haemoglobin more so higher affinity
So haemoglobin has a high % saturation to oxygen

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
10
Q

Where does oxygen mostly load onto haemoglobin?

A

In the alveoli in the lungs because a high partial pressure of oxygen
Oxygen diffuses into blood from alveoli into blood

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
11
Q

Trend for oxygen unloading from haemoglobin

A

Where there is a low partial pressure for oxygen, oxygen will unload from haemoglobin
So less affinity
And lower % saturation of haemoglobin with oxygen

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
12
Q

Where does oxygen unload from haemoglobin?

A

In respiring tissues where oxygen has been used in respiration so has a low partial pressure of oxygen into cells

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
12
Q

Affinity for oxygen in lungs

A

High

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
13
Q

Affinity for oxygen in respiring tissues

A

Low

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
14
Q

Partial pressure of oxygen

A

A measure of oxygen concentration in a given volume caused by oxygen molecules colliding which exerts pressure

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
15
Q

Dissociation curve

A

Shows the % saturation of haemoglobin with oxygen on y axis
Partial pressure of oxygen on x axis
Thus overall affinity oxygen has to haemoglobin at various pO2

16
Q

Shape of a dissociation curve

A

S shaped

17
Q

Why is the dissociation curve or haemoglobin not linear and S shaped?

A

Due to the structure of haemoglobin and the 4 binding sites of oxygen: as more oxygen binds, tithe affinity for oxygen decreases

18
Q

Steep S shaped part of dissociation curve ?

A

When 1 oxygen binds to a haem group, the shape of haemoglobin (tertiary structure) alters to make it easier for more O2 to bind thus for a small increase in pO2, the % saturation increases rapidly

19
Q

Bohr effect

A

The partial pressure of CO2 in a cell can affect the unloading of oxygen

20
Q

What the sigma?

A

GUMMY!!!!!!!!!

21
Q

Effect of increasing pCO2

A

Haemoglobin unloads easily
So at a given partial pressure of oxygen, there is a lower % saturation of haemoglobin with oxygen

22
Q

Effect of increasing pCO2 on the graph

A

Shifts right

23
Q

Effect of decreasing pCO2

A

There is higher affinity for oxygen so oxygen doesn’t unload from haemoglobin easily

24
Q

Effect of decreasing pCO2 on the graph

A

Shifts left so for any given pO2, the % saturation haemoglobin has of oxygen is higher (so lower affinity)

25
Q

What factors can affect the type of haemoglobin in an organism (thus affinity for O2)

A

Oxygen level in environments
Activity levels
Size

26
Q

Animals which live in environments with low oxygen levels?

A

Haemoglobin has high affinity for oxygen compared to living in normal pO2 environments
So it can bind to any available oxygen so high % saturation for a given pO2

27
Q

Effect on the graph of living in low pO2 environments

A

Shifts left so for a given partial pressure, higher affinity for oxygen for given pO2

28
Q

Animals with high activity levels?

A

Have high activity have a higher demand for oxygen thus need a lower affinity for oxygen at a given pO2 so more oxygen unloaded to respiring tissues

29
Q

Effect on the graph of animals with high activity levels

A

Shifts right for a given partial pressure, the % saturation of oxygen is lower

30
Q

Animals that are smaller effect?

A

Higher sa:vol ratio so lose heat easily
More metabolic rate to maintain body temp so higher demands for O2
So for a given pO2, the affinity to oxygen is lower