haemoglobin Flashcards

1
Q

what does haemoglobin do?

A

● loads O2 (at lungs to form oxyhaemoglobin)

● oxyhaemoglobin carries O2 to respiring cells

● unloads O2 at respiring cells (reforms haemoglobin)

● quaternary protein with associated iron (Fe2+) containing haem groups

● protein found in rbc

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2
Q

explain lungs / alveoli

A

● PALS

● high ppO2 (high conc of oxygen)

● high affinity (more likely to be loading O2)

● loading

● saturated (more O2 molecules loaded)

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3
Q

explain respiring cells

A

● PALS

● low ppO2 (low conc of oxygen)

● low affinity for O2

● unloading

● less saturated

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4
Q

what is the shape of the ODC?

A

sigmoidal curve

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5
Q

what does the steep part of the ODC mean?

A

● going up - deoxygenated blood - O2 is being loaded

● going down - oxygenated blood - O2 is being unloaded

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6
Q

what is cooperative bonding?

A

● loading of first oxygen changes tertiary structure of haemoglobin

● exposes second haeme group binding site

● increases affinity of haemoglobin - second O2

● loads more readily

● reason why ODC is a sigmoidal curve

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7
Q

what is the bohr shift?

A

● changes in oxygen dissociation curve as a result of carbon dioxide levels

● in the presence of CO2, Hb has a lower affinity for O2

● so dissociates from haemoglobin more readily

● by decreasing blood pH

● the saturation of Hb decreases

● O2 is more readily available to respiring cells

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8
Q

how does pCO2 affect affinity for Hb loading / unloading?

A

● at high pCO2, Hb unloads more readily

● good as usually high CO2 near respiring cells which need more O2

● a high pCO2 causes a shift of the odc to the right - known as the bohr shift

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9
Q

explain haemoglobin affinity for O2 at different partial pressures

A

● at same ppO2 haem = more saturated
higher affinity for O2 at any ppO2

e.g. lugworm:

in low ppO2 environment
needs to have high affinity
haemoglobin loads more readily
left shifted

● at same ppO2 haem = less saturated
lower affinity for oxygen at any partial pressure
(right shifted)

● e.g. hummingbird:

lots of muscular contractions
so needs lots of ATP
from aerobic respiration
oxyhaemoglobin unloads more readily
more oxygen to respiring cells
higher rate of respiration

● e.g. field mouse:

high metabolic rate
due to high SA:V ratio
meaning heat lost at a higher rate
heat replaced during respiration (exothermic)
oxyhaemoglobin unloads more readily
more oxygen to respiring cells
higher rate of respiration

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10
Q

what is a quaternary protein?

A

more than 1 polypeptide chain

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11
Q

what is the formula for percentage saturation?

A

oxygenated haemoglobin / maximum saturation x 100

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