lecture 17 - respiratory system 4 Flashcards

transport of gases in blood

1
Q

oxygen diffusion

A

enters blood from the alveoli moving from high to low concentration

in arterial blood it travels to the tissues where it diffuses into the cells

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2
Q

carbon dioxide diffusion

A

made in the tissues

much lower gradient - sufficient to drive the transfer

dropped off at the lungs

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3
Q

what does oxygen do after moving out of the alveoli?

A

moves into the plasma - some remains dissolved but most moves into RBCs where its bound to haemoglobin

RBCs move around the body until it reaches an area where its needed

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4
Q

what happens when haemoglobin reaches an area where oxygen is needed?

A

haemoglobin and oxygen dissociate

O2 is released and dissolves back into plasma and moves into the cells where its required

O2 carrying capacity of haemoglobin can be modified to match O2 delivery to demand

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5
Q

what is the maximum saturation we find in the lungs?

A

100 mmHg of PO2

doesn’t ever quite reach 100% saturation

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6
Q

what does a oxygen dissociation curve tell us?

A

at high PO2 there is very little change in the saturation for a big change in O2
• lung concentrations of O2

at low PO2 there is a steep relationship
• small changes have a big effect on saturation
• tissue concentrations of O2

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7
Q

what does the steepness of an O2 dissociation curve tell you?

A

speed - has to be a quick reaction to unload O2 quick enough

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8
Q

haemoglobin in the lungs and arterial blood

A

fully saturated

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9
Q

haemoglobin at rest

A

PO2 arterial blood: 100mmHg
PO2 tissue level: 40mmHg

25-30% of O2 dissociates from HbO4 - rest of it stays bound and goes back to the lungs

large carrying capacity

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10
Q

haemoglobin during exercise

A

PO2 arterial blood: 100mmHg
PO2 tissue level: 15-40mmHg

85% O2 dissociated from HbO4

exercise increases cellular respiration which increases CO2 and H+ production - pH decreases

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11
Q

effect of PCO2 on O2 saturation curves

A

increased PCO2 moves curve to the right

decreases moves it to the left

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12
Q

effect of pH on O2 saturation curves

A

if you increase pH curve moves to the left
• decrease H+

if you decrease pH curve moves to the right
• increase H+

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13
Q

what does a shift to the left on an O2 dissociation curve show?

A

shows a higher binding affinity

O2 is bound more tightly so stays associated longer

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14
Q

what does a shift to the right on an O2 dissociation curve show?

A

shows a lower oxygen binding affinity

haemoglobin is more likely to drop O2 off

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15
Q

process of CO2 diffusion into RBCs

A

1) CO2 in plasma diffuses into RBC where it reacts with H2O to make carbonic acid by carbonic anhydrase
2) carbonic acid dislocates into H+ and HCO3-
3) HCO3- diffuse out into plasma
4) negative moves out so Cl- moves in to keep charge balance
5) H+ displaces oxygen from haemoglobin to release O2

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16
Q

what is Cl- moving in called?

A

chloride shift

17
Q

what is the Bohr effect?

A

Hb•4O2 + H+ –> HHb+ + 4O2

describes the reduction in oxygen affinity of haemoglobin when pH is low and the increase in affinity when the pH is high

18
Q

what forms does haemoglobin exist in?

A

tense

relaxed

binding of H+ to the global chains of haemoglobin favours the tense formation

19
Q

tensed haemoglobin

A

deoxygenated

global chains are tightly packed and pockets are narrowed necked so oxygen can’t get in

once 1 oxygen binds, it causes a conformational change and opens up the spaces slightly

pockets open and allow oxygen in

cooperative binding of oxygen

20
Q

relaxed haemoglobin

A

oxygenated

21
Q

effect of temperature on O2 dissociation curves

A
increase in temperature 
• increased O2 release at any one PO2 
• curve moves to right 
• decreased affinity
• decreased O2 binding 
decrease in temperature 
• decreased O2 release at any one PO2 
• curve moves to left 
• increased affinity
• increased O2 binding 

exercise increases core temperature - increase oxygen delivery to the muscles

22
Q

effect of 2,3-DPG on O2 saturation curve

A

LONG TERM ADAPTATION

important adaptive mechanism to match O2 demand to delivery

2,3-DPG produced by RBCs interacts with beta chains of haemoglobin causing a conformational change which promotes dissociation of oxygen

at any PO2 more O2 is released from Hb in the presence of 2,3-DPG

improves O2 delivery to tissues which might otherwise become hypotonic

23
Q

how do RBCs produce 2,3-DPG?

A

don’t have mitochondria so no oxidative mechanism or ATP production

produce energy by glycolysis - 2,3-DPG is a side product of glycolysis

24
Q

anaemia and O2 saturation curve

A

total oxygen content of blood is reduced - less Hb

O2 curve shifts to the right
• O2 easily dissociates from Hb - reduced saturation point
• occurs at high PO2 than normal
• due to increased 2,3-DPG concentration

25
Q

factors that affect O2 dissociation curve

A
C - CO2 
A - acid or anaemia 
D - diphosphoglycerate 
E - exercise 
T - temperature 

increase in any of them causes a shift to the right

26
Q

foetal haemoglobin

A

curve shifts left

made of 2 alpha and 2 gamma globins

has a higher affinity for O2 than maternal Hb

not affected by 2,3-DPG as has no beta chains

27
Q

what 3 ways are CO2 transported by in the blood?

A

dissolved in plasma

bound to Hb

as HCO3 in plasma

28
Q

CO2 dissolved in plasma

A

7%

CO2 has a high solubility in plasma

29
Q

CO2 bound to Hb

A

23%

CO2 + Hb = carbaminohaemoglobin

30
Q

CO2 as HCO3 in plasma

A

70%

CO2 + H2O –> H2CO3 –> HCO3 + H+

HCO3 exits RBC in exchange for Cl- anion (chloride shift)

31
Q

what happens if tissue [CO2] is higher than [CO2] in blood?

A

CO2 + H2O –> H2CO3 –> HCO3 + H+

results in bicarbonate and hydrogen ion formation

32
Q

what happens if blood [CO2] is higher than [CO2] in alveoli?

A

CO2 + H2O

33
Q

carbon monoxide and Hb

A

CO binds tightly but reversibly to the iron in Hb forming carboxyhemoglobin

affinity of Hb for CO is 200x than of O2

34
Q

2 effects of CO on O2 dissociation curves

A

limits the amount of oxygen than haemoglobin can carry
• competes for Hb molecule
• plateau of curve moves down

binds and shifts haemoglobin to the relaxed conformation
• O2 is more tightly bound and not dissipated at low PO2 in tissues
• curve changes to hyperbola and shifts left

35
Q

CO poisoning treatment

A

hyperbaric oxygen therapy

facilitates dissociation of CO from Hb