Haemoglobin Flashcards

1
Q

How is haemoglobin a tetramer

A

Made up of 4 monomers 2-alpha and 2-beta

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2
Q

What is the purpose of myosin

A

Monomeric haem protein found in muscle tissue.
Facilitates oxygen transport in rapidly respiring muscle.
Receives oxygen from hb.

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3
Q

What is the shape of the oxygen saturation curve does hb have?

A

Sigmoidal (s-shaped)

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4
Q

What is cooperative binding?

A

If its affinity for its ligand changes with the amount of ligand already bound.

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5
Q

What are the two states of hb

A

T-state (deoxyhaemoglobin) and R-state (oxyhaemoglobin)

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6
Q

Why does Hbf have a higher affinity for oxygen the Hba

A

It takes oxygen from Hba so it has to have a higher affinity.

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7
Q

What is the Bohr effect?

A

A reduction in the affinity for oxygen of haemoglobin when pH decreases (increases in CO2, carbonic acid formed decreases pH)

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8
Q

What is 2,3-BPG and what does it do

A

2,3-bisphosphoglycerate, lowers affinity for oxygen of Hb by stabilising the Hb T state

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9
Q

What is different between sickle cell hb and normal hb

A

In the b subunit of sickle cell, at the 6th position (near outside, on surface of protein) a glutamic acid (glutamate) is replaced with a valine. Valine is non polar and so while on surface of protein it creates a hydrophobic region that will polymerise with other hb molecules.

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10
Q

How do the subunits within hb change during foetal development/after birth

A

Gamma subunits replaced by B-subunits

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11
Q

How is haem involved in hb structure?

A

Stabilsed between helices E (distal histidine) and F (proximal histidine).
The distal histidine in the E helix stabilises the O2 bound form and helps to destabilise the CO bound form

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12
Q

How does oxygen binding cause a conformational change in hb structure?

A

It induces the movement of the Fe ion towards the haem plane
Then induced movement of the F helix
This helps facilitate the allosteric transition of t-state to r-state

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13
Q

How does hb carry CO2

A

It forms carbaminohaemoglobin when CO2 reacts with the Hb n-terminus (produces carbamino terminal residues)

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14
Q

How is CO2 transported in the blood

A

Mostly as HCO3-, CO2 can react with water to form carbonic acid (which dissociates) catalysed by carbonic anhydrase; this reaches the lungs and the same enzyme catalyses the reverse reaction.
Also CO2 can react with the N-terminus of hb to produce carbamino terminal residues/carbaminohaemoglobin

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15
Q

How does Hb carry H+ ions

A

As a buffer does

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16
Q

How does BPG lower hb’s affinity for oxygen

A

Binds to pocket in HB tetramer, prevents conversion of T-state to R-state

17
Q

What can lead to anaemia?

A

Low Fe intake

18
Q

What is porphyria

A

Defect in synthesis of haem group

19
Q

What is thalassemia

A

Reduced synthesis of a or B chains

20
Q

What can blood HBA1c show

A

HBA1c is glycosylated hb, indicative of high blood sugar so can show how effective insulin has been at regulating diabetes I.

21
Q

What are the states of hb

A

T-state

R-state (more likely to me saturated)