Haemoglobin Flashcards

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1
Q

How is the red blood cell adapted?

A

bi-concave shape ( increases SA: VOL and short diff. pathway)

contains only haemoglobin ( which increases O2 capacity)

flexible (can bend through narrow capillaries)

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2
Q

Describe the four structures of a red blood cell

A

primary= sequence of amino acids in the four polypeptide chains

secondary=each chain coiled into a helix

tertiary= filed into precise shape essential for its function

quarternary= all polypeptides link to form an almost spherical molecules, each polypeptide is associated with a beam group ( Fe2+)

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3
Q

How many o2 molecules per HB molecule?

A

4

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4
Q

Where does Loading/associating occur?

A

in the lungs

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5
Q

Where does unloading/dissociating occur?

A

in the tissue

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6
Q

What does ‘high affinity’ mean?

A

it can uptake o2 easily but releases it less easily

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7
Q

What is the role of HB?

A

to transport oxygen

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8
Q

How does the HB molecules adapted to different oxygen partial pressures?

A

it can change its affinity

by changing its 3 in the presence of substances eg. co2
in co2 it binds to the o2 more loosely so o2 can be released

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9
Q

Why are there different haemoglobins?

A

different amino acid sequence

different oxygen-binding properties

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10
Q

What is an erythrocyte?

A

red blood cell

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11
Q

The oxygen dissociation curve for haemoglobin shifts to the right during vigorous exercise.

Explain the advantage of this shift.

A

Lower affinity for oxygen / releases more oxygen / unloads more readily;
(To) muscles / tissues / cells
(For) high / rapid respiration

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