Haemoglobin Structure And Function Flashcards

(43 cards)

1
Q

What is haemoglobin made up of?

A

2 alpha and two beta chains

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2
Q

How much of RBCs is comprised of a globular haemoprotein

A

1/3

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3
Q

What is a haemoprotein?

A

A group of specialised proteins that contain haem as a tightly bound prosthetic group

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4
Q

What is haem a complex of?

A

Protoporphyrin IX and ferrous iron Fe2+

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5
Q

How is the iron held in the centre of the haem molecule?

A

Bonds to the 4 nitrogens of a porphyrin ring

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6
Q

How much Hb is synthesised in the erythroblasts?

A

65%

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7
Q

How much Hb is synthesised at the reticulocyte stage?

A

35%

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8
Q

What is haemoglobin synthesis stimulated by?

A

Tissue hypoxia (lack of oxygen)

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9
Q

How is Hb synthesis stimulated by tissue hypoxia?

A

Hypoxia causes the kidneys to increase EPO production which increases RBC and Hb production

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10
Q

What does EPO Stand for?

A

Erythropoietin

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11
Q

What molecule delivers iron to the reticulocyte?

A

Transferrin

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12
Q

Where does synthesis of protoporphyrins take place?

A

In the mitochondria of RBC precursors

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13
Q

What is synthesis of protoporphyrins mediated by?

A

EPO and vitamin B6

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14
Q

Protoporphyrin + iron->

A

Haem

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15
Q

What are the starting reactants in the synthesis of protoporphyrin?

A

Glycine + succinyl CoA

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16
Q

What is the iron stored as if you don’t need it?

A

Ferritin

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17
Q

Where does synthesis of globin happen?

A

In the ribosome and RER

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18
Q

What does proper globin synthesis depend on?

19
Q

How many functional globin chains are there?

20
Q

What are the two clusters of globin called?

21
Q

What genes are in the B-cluster?

A

Beta, gamma, epsilon and delta

22
Q

Where are the B-cluster genes found?

A

On the short arm of chromosome 11

23
Q

What genes are in the A-cluster?

A

Alpha and zeta

24
Q

Where are the A-cluster genes found?

A

Short arm of chromosome 16

25
What types of globulin are found in foetal Hb?
Alpha and gamma
26
What types of globulin are found in adult Hb?
Alpha and beta
27
What are the functions of haemoglobin?
- carry oxygen from the lungs to the tissues - remove CO2 - buffering action- maintains blood pH as it changes from oxyhaemoglobin to deoxyhaemoglobin
28
How many oxygens can one Hb bind to?
Four
29
How long does it take for Hb oxygenation?
Less than 0.1 seconds
30
What happens (physically) to the Hb when it’s oxygenated?
2,3-DPG is pushed out and the beta chains move closer
31
What does DPG stand for?
Disphosphateglycerate
32
What does the amount of o2 bound to hb and released to tissues depend on?
pO2 pCO2 Affinity of hb for O2
33
What does oxygen affinity determine?
The proportion of o2 released to the tissues or loaded onto the cells at a given pressure
34
What is the Bohr effect?
Alterations in the blood pH shifted the oxygen dissociation curve
35
What happens to the oxygen dissociation curve in acidic pHs?
The curve shifts to the right
36
What happens when the oxygen dissociation curve shifts to the right?
Results in an enhanced capacity to release o2 where it is needed
37
What does the normal position of the haemoglobin oxygen dissociation curve depend on?
2,3 DPG concentration Hydrogen ion conc (pH) CO2 in RBC Structure of Hb
38
What are standard conditions for the Hb- O2 dissociation curve?
37 Celsius pH 7.4 BE =0
39
What are the three mechanisms for CO2 transport?
Dissolution in the plasma Formation of carbonic acid Binding to form carbaminohaemoglobin
40
What is oxyhaemoglobin made up of?
Hb and 02
41
What is deoxyhaemoglobin made up of?
Hb - o2
42
What is methemoglobin made up of?
Hb with Fe3+
43
What is carbaminohaemoglobin made up of?
CO2 binds non-covalently to globin chain of Hb