Erythrocyte Structure and Function Flashcards

1
Q

What size are RBCs?

A

6-8 micrometres

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

Why do RBCs not have a nucleus?

A

So that they have more room for haemoglobin

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

What is the structure of haemoglobin?

A

Four protein globin chains (two alpha and two beta chains) each associated with a non-protein haem group containing iron

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

What is the shape of a RBC and what function does this shape serve?

A

Biconcave disc which provides a larger surface area for gas exchange

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

How many molecules of oxygen can bind to one haemoglobin molecule?

A

4

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

How do RBCs fit through small capillaries which are smaller in diameter than the RBC?

A

RBCs have a flexible cytoskeleton to allow them to squeeze through small capillaries

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

Where in the cell is haem synthesised and which vitamin is required in this synthesis process?

A

The mitochondria

Vitamin B12

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

How does adult haemoglobin vary from foetal haemoglobin?

A

Adult haemoglobin has 2 alpha globin chains and 2 beta globin chains. Foetal haemoglobin has 2 alpha globin chains and 2 gamma globin chains

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

In what state is the iron in haemoglobin?

A

Ferrous (Fe3+)

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

What is haemoglobin called when oxygen is bound to it?

A

Ocyhaemoglobin

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

Describe the change in colour of haemoglobin when oxygen is bound compared to when oxygen is not bound.

A

Oxyhaemoglobin is bright red

Haemoglobin without oxygen is darker red

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

What is the function of 2,3-DPG?

A

It allosterically promotes the release of oxygen from haemoglobin by decreasing the affinity of haemoglobin for oxygen

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

How is oxygen taken up by RBCs in the lungs and released by RBCs in the respiring tissues?

A

The affinity of haemoglobin for oxygen is related to partial pressure of oxygen. Affinity is high when partial pressure is high in the lungs (causing binding) and affinity is low when partial pressure is low in the respiring tissues (causing release)

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

In what form is carbon dioxide transported by haemoglobin and how is it changed to this form?

A

Carbon dioxide is converted to bicarbonate by the enzyme carbonic anhydrase in RBCs

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

RBCs respire aerobically. T/F?

A

False - they respire anaerobically via the embden-myerhof pathway

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
16
Q

How many molecules pf ATP are gained by RBCs when they respire?

A

Net gain of ATP = 2

17
Q

What is the lifespan of a RBC?

A

120 days

18
Q

What is triggered by the release of nitric oxide by haemoglobin?

A

Local vasodilation to increase blood flow and oxygen supply to nearby cells.

19
Q

In the Embden-Meyerhof pathway what is glucose converted to?

A

Lactate