[OLD] Haemoglobin Flashcards

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1
Q

Describe the structure of haemoglobin? List at least 3 facts

A

A protein containing 4 polypeptide chains.
Quaternary structure
Each polypeptide contains a haem group, which contains iron

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2
Q

What are the units for partial pressure of oxygen?

A

pO2

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3
Q

What are the terms sometimes used to describe the binding and releasing of oxygen by haemoglobin?

A

loading and unloading

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4
Q

Explain why it is important for haemoglobin to be soluble.

A

so it can be transported in the blood

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5
Q

Red blood cells contain some enzymes. Explain why the enzymes cannot be synthesised in red blood cells.

A

it does not contain a nucleus

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6
Q

4 key points of haemoglobin structure

A

4 interlocking globin subunits
each with a porphyrin ring
contains Fe2+
each ring carries one O2 molecule

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7
Q

advantages of the sigmoidal curve

A

Lower affinity at low partial pressures of oxygen
> unloads oxygen to the tissues more readily

Higher affinity at high partial pressures of oxygen
> more efficient at loading oxygen in lungs

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8
Q

what is the Bohr effect?

A

In a CO2-rich environment (i.e. at respiring tissue), more oxygen dissociates from oxyhaemoglobin

Oxygen dissociation curve shifts to the right

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9
Q

Advantage of the Bohr effect

A

when a muscle is respiring more it receives an increased amount of oxygen.

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10
Q

what in haemoglobin binds to oxygen?

A

the Fe2+ ion in the haem group

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11
Q

how are red blood cells adapted to transport oxygen?

A
no nucleus, Golgi, rer, mitochondria
contains haemoglobin
biconcave shape
flexible membrane
small size
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12
Q

why is binding to the first o2 difficult?

A

low diffusion gradient to haem group in centre of molecule

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13
Q

what does binding of the first o2 do?

A

produces a conformational change in shape

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14
Q

where do foetuses get oxygen from?

A

it’s mothers blood across the placenta

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15
Q

does foetal haemoglobin have a higher or lower affinity for oxygen than adult haemoglobin?

A

higher

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