Haemoglobin Flashcards

1
Q

What is haemogloin

A

Water soluble globular protein

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2
Q

What is the structure of haemoglobin

A

4 polypeptide chains, 2 beta and 2 alpha helices - so quaternary structure
4 associated haem groups as each oxygen binds to the haem ( fe2+ ) group
Each molecule can carry 4 o2 molecules

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3
Q

What is affinity

A

How easily haemoglobin binds to oxygen

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4
Q

What is loading/ association

A

Proscess of haemoglobin binding to oxygen

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5
Q

What is unloading/ disassociation

A

When haemoglobin lets go/ unbinds to oxygen

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6
Q

What is partial pressure

A

How much gas contributes to the pressure ie how concentrated a gas is

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7
Q

What are the 3 factors that affect affinity

A

1: partial pressure of o2
2: oxygen saturation
3: partial pressure of carbon dioxide

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8
Q

How does the partial pressure of o2 affect affinity

A

More oxygen equals higher affinity so more loading occurs

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9
Q

How does oxygen saturation affect affinity

A

Low oxygen: low affinity, difficult to hold, more unloading
High oxygen: higher affinity, easier to load ,more loading

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10
Q

How does partial pressure of co2 affect affinity

A

More co2 means lower affinity so more unloading

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11
Q

What happens when you increase co2 in the blood
-ph
- respiring cells
- tertiary structure
- aerobic respiration
- delays

A
  • increasing co2 in the blood will decrease the ph
  • decrease in ph will affect the tertiary structure slightly
  • lowering affinity so more o2 unloading or aerobic respiration therefore more energy from atp
  • more o2 unloading delays anaerobic respiration so less lactic acid is produced and less cramps
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12
Q

Describe and explain the advantage of the Bohr effect during intense exersise

A
  • increased unloading of o2
  • carbon dioxide reduces ph of blood so changed shape of hb
  • more oxygen for aerobic respiration
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13
Q
A
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