3.3.4.1 Mass transport in animals Flashcards

(10 cards)

1
Q

describe the structure of haemoglobin

A

a protein with a quaternary structure - made up of 4 polypeptide chains. each chain has a haem group containing an iron ion

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2
Q

where is haemoglobin found?

A

in red blood cells

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3
Q

how many oxygen molecules can a human haemoglobin carry?

A

each molecule of human haemoglobin can carry 4 oxygen molecules

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4
Q

what is the role of haemoglobin in the body?

A

to carry oxygen around the body

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5
Q

how is oxyhemoglobin formed?

A

when oxygen in the lungs binds to the iron ion in the haem groups within the haemoglobin

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6
Q

where is oxyhemoglobin formed?

A

in the lungs

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7
Q

when does oxygen leave the oxyhemoglobin?

A

oxygen leaves the oxyhaemoglobin near the body cells turning it back to haemoglobin

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8
Q

what is the process called in which an oxygen molecule binds to the iron ions in haemoglobin?

A

association / loading

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9
Q

what is the process called in which oxygen leaves the oxyhaemoglobin?

A

dissociation / unloading

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10
Q
A
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