Haemoglobin Flashcards

1
Q

Where is it found

A

Red blood cells(erythrocytes)

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2
Q

structure of haemoglobin

A

It is a quaternary structured protein as it is made of 4 polypeptide chains . Each polypeptide chain contains a haem group containing iron ion which combines to oxygen.

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3
Q

How does haemoglobin load and unload oxygen

A

Haemoglobin can carry 4 oxygen molecules one at each haem group. In the lungs , at a high partial pressure haemoglobin has a high affinity for oxygen and as a result it readily associates with haemoglobin. At respiring tissues at a low partial pressure oxygen dissociates from haemoglobin.

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4
Q

Bhor effect

A

As concentration of CO2 is high the rate of unloading is faster. This is advantageous as it provides more oxygen for respiring tissue that are undergoing aerobic respiration

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5
Q

Importance of ion

A

Iron ion—> allows oxygen molecule to bind to haem group
no iron ion = haemoglobin function less efficiently as oxygen wont be loaded into haemoglobin ——-> no oxygen for respiring tissue and muscles.

Knock on effect on mitochondria as they need oxygen to produce ATP through oxidative phosphorylation

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