Haemoglobin Flashcards

1
Q

What is haemoglobin?

A

A large protein with a quaternary structure, that has a high affinity for oxygen. Has 4 polypeptide chains that each has a haem group which contains an iron ion

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2
Q

What is oxyhaemoglobin?

A

The combining of oxygen and haemoglobin

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3
Q

Where does oxygen load onto haemoglobin?

A

Where there is a high partial pressure of oxygen

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4
Q

Where does oxyhaemoglobin unload its oxygen?

A

Where there is a lower partial pressure of oxygen

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5
Q

Why is the dissociation curve an ā€˜Sā€™ shape?

A

When haemoglobin combines to the 1st oxygen molecules it makes it easier for other molecules to join. As saturation increases it gets harder for more oxygen molecules to join

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6
Q

What is the Bohr shift?

A

When the dissociation curve moves to the right because haemoglobin unloads oxygen more easily due to an increase in the partial pressure of carbon dioxide

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7
Q

What organisms will have a high affinity for oxygen?

A

Organisms that live in environments with a low concentration of oxygen

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8
Q

What organisms will have a low affinity for oxygen?

A

Organisms that are very active and have a high oxygen demand

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