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Biology > Section 3- Haemoglobin > Flashcards

Section 3- Haemoglobin Flashcards

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1
Q

What is the structure of haemoglobin?

A

Globular protein with a quaternary structure
(4 polypeptide chains)

4 chains= 2 alpha chains, 2 beta chains

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2
Q

What part of the haemoglobin binds to an oxygen molecule?

A

The prosthetic group- contains a iron ion

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3
Q

What is created when oxygen binds to haemoglobin?

A

Oxyhaemoglobin (HbO8)

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4
Q

Why is oxygen binding and unbinding a reversible reaction?

A

Oxygen is LOADED in the lungs and UNLOADED in the tissues

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5
Q

What is the process by which haemoglobin bind and unbinding with oxygen is called?

A

Loading or associating

Unloading or dissociating

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6
Q

What is cooperative binding?

A

When a molecule of oxygen binds to haemoglobin, it changes the tertiary structure slightly revealing other binding sites

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7
Q

Haemoglobins with a high affinity for oxygen…

A

take up oxygen more easily, but release it less easily

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8
Q

Haemoglobins with a low affinity for oxygen…

A

take up oxygen less easily, but release it more easily

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9
Q

What is the affinity for oxygen affected by?

A

The partial pressure of oxygen in the tissues surrounding the haemoglobin

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10
Q

What is the role of haemoglobin?

A

Transport oxygen

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11
Q

To be efficient at transporting oxygen, haemoglobin must…

A
  • readily associate with oxygen at the surface where gas exchange takes place
  • readily dissociate from oxygen at tissues requiring it
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12
Q

How does DNA lead to different haemoglobin molecules having different affinities for oxygen?

A

Different base sequence
Different amino acid sequence
Different tertiary and quaternary structure and shape
Different affinities for oxygen

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13
Q

Why might a person breathing in car-exhaust fumes lose consciousness?
(When carbon monoxide binds permanently to haemoglobin in preference to oxygen)

A

Carbon monoxide will occupy all site of haemoglobin instead of oxygen
No oxygen will be carried to tissues (brain)
Cease to respire and to function
Person loses consciousness

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14
Q

What shape is an oxygen dissociation graph?

A

S (sigmoid shape)

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15
Q

In the lungs where the partial pressure of oxygen is high…

A

Haemoglobin has a high affinity

Loads or associates with lots of oxygen

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16
Q

In the tissues with a low respiration rate, the partial pressure of oxygen…

A

Is relatively low

The affinity for oxygen decreases

17
Q

In tissues with a high respiration rate, the partial pressure of oxygen is…

A

Much lower

18
Q

How does the partial pressure of carbon dioxide affect oxygen-haemoglobin binding?

A

As partial pressure of CO2 increases, conditions are more acidic- haemoglobin changes shape.

The affinity of haemoglobin for oxygen decreases
Oxygen is released from haemoglobin
THE BOHR EFFECT

19
Q

How does partial pressure of oxygen affect oxygen-haemoglobin binding?

A

As partial pressure of oxygen increases, the affinity of haemoglobin for oxygen increases
Oxygen binds tightly to haemoglobin

When partial pressure is low, oxygen is released from haemoglobin

20
Q

What acid is produced when CO2 dissolves into blood plasma and reacts with water?

A

Carbonic acid

21
Q

Why does the oxygen dissociation curve steeply increase?

A

The 2nd and 3rd oxygen molecules bind easily to the haemoglobin.

22
Q

How is the affinity for oxygen affected when the oxygen dissociation curve is further to the left?

A

Greater affinity of haemoglobin for oxygen

Loads oxygen readily but unloads less easily

23
Q

What is the Bohr effect?

A

The greater the concentration of carbon dioxide, the more readily the haemoglobin releases it oxygen

24
Q

When a tissue is more active, more oxygen is unloaded. Why?

A 
Higher rate of respiration
More carbon dioxide is produced by tissues
Lower pH
Greater haemoglobin shape change
More readily oxygen is unloaded
More oxygen is available for respiration
25
Q

What effect does a change in tertiary structure have with oxygen affinity?

A

Affinity for oxygen will be lower

More oxygen is unloaded

26
Q

How has haemoglobin adapted in low oxygen environments?

A

Haemoglobin becomes fully saturated at lower partial pressure of oxygen
Higher affinity for oxygen

Fully saturated at much lower partial pressure of oxygen

27
Q

How has haemoglobin adapted with highly active animals?

A

Haemoglobin has a lower affinity for oxygen
Unloads much quicker to respiring tissues
Decrease in partial pressure
More oxygen to respiring tissues

28
Q

How has haemoglobin adapted in animals with a large surface area to volume ratio?

A

High metabolic rate, requires more oxygen

Higher partial pressure

Respiring tissues get more oxygen

29
Q

How does a rise in temperature enable an exercising muscle to work more efficiently?

A

Exercising muscles release heat
Shifts curve to the right
Haemoglobin releases more oxygen to fuel muscular activity

30
Q

How do you calculate percentage saturation of haemoglobin with oxygen?

A

(Oxygenated Hb / Maximum saturation) X 100

31
Q

What enzyme catalyses the reaction where carbon dioxide diffuses diffuses into the red blood cells?

A

Carbonic anhydrase

32
Q

What is the advantage of foetal haemoglobin having a different dissociation curve from maternal haemoglobin?

A

Higher affinity at lower partial pressure.

Able to become fully saturated with oxygen from mothers blood.

Foetus has high respiration so needs lots of oxygen.

33
Q

When hydrogen ions combine with haemoglobin, they form a compound known as…

A

haemoglobinic acid

34
Q

What enzyme catalyses the reaction leading to the production of hydrogen ions and hydrogen carbonate ions after the diffusing of CO2 into the red blood cells?

A

Carbonic anhydrase

Biology (25 decks)

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