Haemoglobin Flashcards

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1
Q

Why does haemoglobin have a quarternary structure

A

4 polypeptide chains

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2
Q

What is a haem group

A

Iron

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3
Q

What affinity for oxygen does haemoglobin have

A

High

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4
Q

What is oxygen partial pressure

A

Oxygen concentration

The amount of pressure oxygen atoms exert in a total volume of gas

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5
Q

When does haemoglobin load oxygen

A

High oxygen partial pressure

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6
Q

When does haemoglobin unload oxygen

A

Low partial pressure of oxygen

Eg. High CO2 partial p

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7
Q

Give an example of when haemoglobin has a high affinity for oxygen

A

Lungs

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8
Q

Give an example of when haemoglobin has a low affinity for oxygen

A

Repairing muscle cells

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9
Q

What shape is the oxygen dissociation curve

A

Sigmoid

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10
Q

Why is the oxygen dissociation curve a sigmoid shape

A
1 = hard = polypeptide chains bound tightly. Binding sights are no exposed 
2/3 = easy = bases are exposed
4 = hard = due to probability it is unlikely it will bind
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11
Q

Explain why there is low saturation at low partial p

A

Haemoglobin has a low affinity for oxygen
Oxygen readily unloads
Eg. Muscle cells

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12
Q

Explain why there is a high saturation at high partial p

A

Haemoglobin has a high affinity for oxygen
Readily loads oxygen
Eg. Alveoli

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13
Q

Explain the Bohr effect

A

Respiring cells have high partial p of CO2
Shifts position of curve to the right
At a higher p(O2) the saturation is lower
Oxygen more readily unloads (has a lower affinity)

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14
Q

What position does the curve shift in high p(CO2)

A

Right

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15
Q

Which way does the curve shift in high p(O2)

A

Left

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16
Q

Which way do animals who live in low levels on O2 curve shift and why

A

Left
Need haemoglobin with a higher affinity for oxygen in lower pp
So at a lower pp the saturation is higher

17
Q

Which way do very active animals curve shut and why

A

Right
High oxygen demand at respiring cells
Need haemoglobin with lower affinity for O2
So at a high pp the saturation is lower