8.4 transport of oxygen and carbon dioxide

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features of erythrocytes

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33 Terms

1

features of erythrocytes

  • biconcave disc

  • no nucleus

  • contains haemoglobin

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2

functions of erythrocytes

  • pass through narrow capillaries

  • maximise amount of haemoglobin due to no nucleus

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3

structure of haemoglobin

  • globular conjugated protein

  • four peptide chains

  • each chain contain iron-containing prosthetic group

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4

how is oxyhaemoglobin formed

  • oxygen bonds loose with haemoglobin

    Hb + 4O2 Hb(O2)4

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5

how is there a steep conc grad between erythrocytes and alveoli

  • oxygen levels relatively low in erythrocytes when enter capillaries in lungs

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6

what happens after one oxygen molecule binds to a haem group

molecule changes shape, making it easier for the next oxygen molecules to bind

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7

what is positive cooperativity

when oxygen molecules binding makes it easier for others to bind

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8

what happens when blood reaches body tissues

conc of oxygen in erythrocytes higher than cytoplasm

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9

what does an oxygen dissociation curve show

affinity of haemoglobin for oxygen

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10

what is the shape of the oxygen dissociation curve

S shape

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11

why is the oxygen dissociation curve that shape

  • increase partial pressure of oxygen

  • easier for other oxygen molecules for bind

  • levels off as haemoglobin is saturated

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12

what happens to haemoglobin at low pO2

haem groups bound to oxygen so haemoglobin does not carry much oxygen

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13

what happens when pO2 is increased

haem groups are bound to oxygen, making it easier for more oxygen to be picked up

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14

what happens when the pO2 is very high

haemoglobin is saturated as all haem groups become bound

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15

what is the bohr effect

when haemoglobin gives up oxygen more easily

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16

why does the bohr effect happen

partial pressure of carbon dioxide rises

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17

result of the bohr effect

  • in active tissues with high pCO2, haemoglobin gives up oxygen more readily

  • in lungs where proportion of CO2 in air relatively low, oxygen bind to haemoglobin molecules easily

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18

what happens to the oxygen dissociation curve when the bohr effect happens

curve shifts to the right

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19

why does fetal haemoglobin have a higher affinity for oxygen than mother

so it can remove oxygen from the maternal blood so oxygen can be transferred to the blood of the fetus

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20

how is the fetal dissociation curve differ from normal

fetal dissociation curve is moved to the left

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21

three ways carbon dioxide is transported from tissues to lungs

  • dissolved in the plasma (5%)

  • combined with amino groups in haemoglobin to form carbaminohaemoglobin (10-20%)

  • converted to hydrogen carbonate ions (75-85%)

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22

chemical formula of hydrogen carbonate ions

HCO3-

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23

how does CO2 enter RBC

diffusion

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24

how does CO2 turn into H2CO3 (carbonic acid)

CO2 + H2O H2CO3 using carbonic anhydrase

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25

what is the enzyme used to form carbonic acid

carbonic anhydrase

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26

what does H2CO3 dissociate into

H+ and HCO3- ions

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27

how do HCO3- ions leave RBC

diffusion into plasma

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28

H+ ions and HbO3 (oxyhemoglobin) form what

4O2 and HHb (haemoglobinic acid)

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29

role of HHb (haemoglobinic acid)

a pH buffer

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30

what happens with the 4O2 produced

diffuse out into plasma

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31

what is the chloride shift

Cl- ions diffuse into RBC to maintain neutral charge

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32

what is the effect on RBC charge when ions diffuse out

RBC becomes positively charged until Cl- ions diffuse in

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33

when will the HCO3- reactions reverse

when there is a relatively low concentration of carbon dioxide in the lung tissue

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