topic 4.5 - transport of gases in the blood Flashcards

You may prefer our related Brainscape-certified flashcards:
1
Q

what is the main job of haemoglobin

A

to transport oxygen around the body

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

transport of oxygen - how do the molecules bind?

A
  • 1st oxygen molecule that binds alters the arrangement of the molecule
  • easier for the following oxygen molecules to bind
  • final O2 molecule binds a lot faster than first
  • same process in reverse when oxygen dissociates from haemoglobin
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
3
Q

structure of haemoglobin and how it transports oxygen

A
  • haemoglobin is a large globular protein
  • made up of 4 peptide chains, each with an iron containing prosthetic group (haem group)
  • can pick up 4 molecules of O2 in a reversible reaction to form oxyhaemoglobin

Hb + 4O2 ⇌ Hb4O2
haemoglobin + oxygen ⇌ oxyhaemoglobin

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

transport of oxygen - how do the molecules bind? (positive cooperativty)

A
  • 1st oxygen molecule that binds to iron alters the arrangement of the haemoglobin molecule
  • easier for the following oxygen molecules to bind
  • final O2 molecule binds a lot faster than first
  • same process in reverse when oxygen dissociates from haemoglobin
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
5
Q

where is the partial pressure of oxygen high

A
  • the lungs have a high pp of oxygen
  • so oxygen binds rapidly with haemoglobin to form oxyhaemoglobin
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
6
Q

why does the percentage saturation of oxygen in the lungs not reach 100%

A
  • most iron atoms are already bound to the oxygen molecules
  • the probability of a collision between an unbound iron atom and oxygen molecule is low
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
7
Q

oxygen levels in body tissues

A
  • relatively low
  • concentration of oxygen in cytoplasm of RBC is higher than in the surrounding tissue
  • hence, O2 moves out by diffusion down its concentration gradient
  • haemoglobin gives up some of its O2
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
8
Q

Bohr effect

A
  • in the presence of CO2 the affinity of haemoglobin for oxygen decreases so it is released
  • hence, oxygen dissociates from haemoglobin and can be used in respiring tissues
  • changes in carbon dioxide concentration result in changes in the curve - Bohr effect
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
9
Q

Bohr effect - haemoglobin and oxyhaemoglobin dissociation curve - increased CO2

A
  • increase in CO2 causes curve to shift to the right
  • oxygen associates less readily and dissociates more readily
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
10
Q

Bohr effect - haemoglobin and oxyhaemoglobin dissociation curve - decreased CO2

A
  • decrease in CO2 causes curve to shift to the left
  • oxygen associates more readily and dissociates less readily
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
11
Q

what happens when oxygen dissociates from haemoglobin?

A
  • gets harder to remove the oxygen
  • conc of oxygen in RBC when blood enters is low
  • concentration of oxygen in cytoplasm of RBC is higher than in surrounding tissue
  • hence oxygen moves into cells via diffusion down its concentration gradient
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
12
Q

what is myoglobin

A
  • respiratory pigment found in muscle tissue of vertebrates
  • small bright red protein
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
13
Q

structure of myoglobin and how this relates to its function

A
  • similar to a single haemoglobin chain
  • single polypeptide chain
  • contains haem group which binds oxygen
  • has a higher affinity for oxygen so becomes easily saturated
  • once bound to oxygen, it doesn’t give up oxygen easily hence acts as an oxygen store
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
14
Q

similarities between haemoglobin and myoglobin

A
  • both globular proteins
  • both contain haem group/s
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
15
Q

differences between haemoglobin and myoglobin

A
  • higher oxygen affinity in Mb
  • haemoglobin carries oxygen to cells in body whereas Mb stores oxygen in muscle cells to be used as energy
  • Hb has quarternary structure, Mb has tertiary structure
  • higher conc of Hb in blood, higher conc of Mb in heart & muscle cells
How well did you know this?
1
Not at all
2
3
4
5
Perfectly