4.5 Transport of Gases in Blood Flashcards

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1
Q

describe the structure of erythrocytes and how it is adapted for gas exchange

A

biconcave shape - maximises surface area for gas exchange
small + flexible - allows easier movement through narrow capillaries
no nucleus - more room to carry respiratory gases
packing with haemoglobin

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2
Q

what is haemoglobin made up of?

A

4 globular proteins

1 iron ion

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3
Q

give a property of haemoglobin

A

it has an affinity for oxygen - can carry up to four oxygen molecules

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4
Q

what is it called when haemoglobin becomes oxygenated?

give the equation

A

oxyhaemoglobin

Hb + 4O2 « Hb4O2

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5
Q

define partial pressure of a gas

A

amount of gas present in a mixture

measured by the pressure it contributes to total pressure of gases

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6
Q

describe how oxygen is transported in the lungs

A

oxygen diffuses into blood plasma
passes down a concentration gradient + into erythrocytes
oxygen binds to Hb to maintain the conc gradient
oxygen binds to Fe2+ group of Hb

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7
Q

describe how oxygen is transported in the respiring tissue

A

oxygen dissociates from oxyhaemoglobin

oxygen can then diffuse out of the erythrocytes + to respiring cells

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8
Q

what is pO2?

A

partial pressure for oxygen
amount of oxygen in tissue
measured in kPa

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9
Q

what does it mean to have a high partial pressure for oxygen?

A

more oxygen molecules are able to associate with Hb molecules to be transported

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10
Q

where is haemoglobin saturation the highest in the body?

A

in the lungs

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11
Q

in respiring tissue, tje pO2 is low. what happens?

A

at low pO2, oxygen dissociates from oxyhaemoglobin + can diffuse to the respiring cells

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12
Q

as pO2 increases, what happens to the saturation of Hb?

A

increases

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13
Q

describe the process of oxygen associating with haemoglobin

A

after the first oxygen associates, the conformation of Hb changes
conformation change makes it easier for the 2nd and 3rd molecule to associate
it is difficult to associate a fourth oxygen because Hb becomes saturated (“full”)

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14
Q

what do we mean by high affinity?

A

Hb binds more easily, even at low pO2

dissociates less readily

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15
Q

what do we mean by low affinity?

A

Hb binds less readily
dissociates faster
oxygen is readily available for respiring tissue

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16
Q

what is foetal haemoglobin?

A

red blood cells in the foetus contain a special form of Hb

17
Q

which has a high affinity for oxygen, adult or foetal Hb? explain why.

A

foetal Hb - helps to maimise oxygen uptake from mother’s blood, which has already lost some of its oxygen by the time it reaches placenta

18
Q

to get oxygen from maternal blood to foetal blood, what must happen ?

A

foetal Hb needs a stronger affinity for oxygen than maternal Hb

19
Q

give two features of foetal Hb

A

stronger oxygen affinity

becomes saturated at lower pO2

20
Q

describe what myglobin is

A

respiratory pigment found in muscles
small red protein
contains haem group which binds to oxygen

21
Q

give 3 features of myoglobin

A

higher affinity for oxygen than haemoglobin
becomes easily saturated with oxygen
not affected by pO2 in tissues

22
Q

what happens when myoglobin binds to an oxygen molecule?

A

it does not give up easily so acts as an oxygen store

when o2 levels in active muscles get low, and co2 levels are high, myoglobin releases its store of o2

23
Q

give differences in structure and affinity to o2 of haemoglobin and myoglobin

A

Hb-
tetramer- 4 polypeptide chains
supplies blood all over body
low affinity to o2 compared to Mb

Mb-
monomer- 1 polypeptide chain
supplies o2 to muscles
higher affinity to o2 compared to Hb

24
Q

what is the Bohr effect?

A

effect of co2 on oxygen dissociation on Hb curve

25
Q

at high carbon dioxide levels in tissues

A

Hb binds with O2 less well (low affinity) so releases more o2

26
Q

at low carbon dioxide levels in lungs

A

Hb binds with oxygen more easily (high affinity)