4.2 Oxygen dissociation curve Flashcards
Draw Oxygen dissociation curve - normal adult hb
What points Id w/ normal values
Why is it sigmoid
page 122
Hba one
Three main points -
Arterial point Po2 Sat O2 97.5 13.3kPa
Mix venous = 5.3
p50 3.5
Sigmoid - positive cooperativity
What is the mix venous point
Mix venous blood
Po2 here 40mmHg -
Hb sats 75%
Oxygen content - not specified without further info
Note mix venous point not like odc
increase poc2 and ph in mix venous means that mex venous point lies on a right shift ODC - bohr effect
What is meant by p50
What is it
What is it used for
why was point on curve chose
Reference oxygen dissoc curve - pp o2 - 50% sat carry protein
Normal p50 3.5
P50 - specify position oxygen on o2 dissoc curve - index of affinity of oxygen carrying protein
Most useful to specify curve positon becuase its on steepest point on curve most sneistive for detecting shif of curve
allows comparison position other curves under diff conditions
What does a right shift indicate
decrease oxygen affinity - p50 high for right hsift
Causes by 4 things
Tempertue
[H+]
pCO2
Red cell 2 3 DPG level
Superimpose curve HBf
Why is it that way
page 123
Left shifted - compared hba - cause lower binding 2 3 dpg by Hbf
Simgoid - similar to normal oDC but slightly left shift
lower by 2.3kpa
Lower p50 - hgiher oxygen affinity
reduced bind 2 3 dpg to feoteal hb
2 3 dpg binds best to beta chain adult hb - right shift decrease affinity
2 3 binds avdily to beta of deoxy
foeteal 2 alpha 2 gamma
no beta
- coneseq lower p50
Draw oxygen didsociaton curve with oxygen content on y axis
page 124
mls dlo
What is myoglobin
Draw oxygen dissoc for myoglobin
explain shape
whats the advantage of shape
Haem contain oxygen binding protein
present skeletal muscle - role oxygen store
page 125
Rectangular Hyperbolic shape
vlow p50 .36
Lies very left of sigmoid hb curve
high affinity
advantage
ptake oxygen from hb
load and unload of range po2 in cell
if p50 could never load oxygen
intracellular po2 - vary diff cells
typically low
ox phosp cease <1mmhg
myoglob with its low p50 well match intracellular needs muscle cell
load oxygen from hb
unload to cell as cytoplasmic po2 falls low
Chemical reason
different structure
myoglob single globin chain
dissoc curve rectang hyperobla
hb contain globin chain an doxygenation of each casues struct change w. increasing affinity of haem for reamins oxygen
subunit interaction positive cooperativity - increase oxygen affinity as load - causes sigmoid shape of curve
What is physiological signifcane of shape of oxy dissoc curve for adult hb
1 Flat upper part
act buffer -s ense po2 drop to about 10.6kpa yet hb remain saturate 96% with oxygen
keeps arterial oxygen conc high despiate impair sturation lung
keeps large pp diff b/w alveoli and capillary after most o2 transferred
2 Steep part curve
Tissue reqire more oxygen large amounts of oxygen can be removed wihtout much further drop in po2
Pressure grad for diffsuion from capillary to cell - welle mintainted despite increased oxygen extraction
Summary shpae odc
Double buffering because
flat upper part buffer hb sat against substatn drop in po2 - useful maintain art hb sat
steep part large o2 unloading and main o2 diffison graduiaton
How is saturation of hb definied
oxy sat = actual content of Hb x 100
_______________________________
Max oxygen content of hb
What is the effect of acute anaemia on ODV
Curve not alter if sat on y vs po2 on x
If drawn as oxygen cconent versus po2 - p2 halved - shape not alrered
in chronic anaemia 2 3 dpg rises and right shfits
What is affect of Carbon monoxide on ODC
1 Curve is LEFT shifted
2 o2 content reduced
Left shift - binding co conformational change in hb - increased affinity for oxygen in oher subunits
How is carboxyhb dissoc curve diff from two curve
draw curve
dissoc CO from HB - cruve dissoc of oxygen for Hb in presence of CO as modifiny
Diffrence -
axes - sat hb CO on yo
PP pCo on x
extremely high affinity for curve mean extreme left shift and rectangular hyperbola
Page 127
Oxygen diddosc curve for Hb in presence of carobxy
draw sat on y - o2 dissoc prsence of CO same shape left shift
reduction in o2 content not apparetn when o2 satus used on y
If drawn with o2 content of hb on Y odc in Carbom monoxide left shift and reduced in size
ex curve draw hb 15g 33% hb co 10g avail combo oxygen - max content is 2/3
Dissoc curve for Hbcvo diff curve
pp co on x and pcc50 very low
What is difference between function sat and fractional saturation? is it clin important
oxgen ssat - function sat
tradition way consider sa
sat cont x 100/capaity
sat hb - determ measure actual oxy coent and measure o2 of another sample after equib room air
but blood may contain 4 hb species
oxyhb deoxy methb cohb only one carries
funct sat hbo2 x 1– / hbo2 + deoxy
Fraction sat
Hb o2 x 100/ total hb
total hb = hb deox met co
Clinically more useful consider fraction sat
large amt met co - function mislead
value displayed pulse oxy neither function or fract
depends on calibration used for brand - may be close to one or other
as a two wavelength limited measure two hb species hbo2 and deoxy
Carbon dioxide transport
Tell me about Co2 tport in blood
what is contribution diff forms tport Co2 carraige and AV difference Co2 content
What is the arterial Co2 Content
Carbon dioxide is carried in 3 forms
1 Dissolved Co2
2 Bic
3 Caarbamino compounds
Art blood contains 48 Co2/dl and mix ven 52
Percentage of and % contrib to AV difference
Dissovled 5 10
Bic 90 60
Carbamino 5 30
What are carbamino compounds
Formed Co2 reacting
1 terminal AA groups proteins
2 Amino groups in side chain arginine and lysine
Hb is more important plasma proteins in formation of carbamino because
1 More hb present 15 v 7
Hb teatremer 4 N terminal groups/molecule & alb has 1
Dormation of carbamino ncrease greatly as Hb becomes doexygenated
what are reactions occurring in systemic capillaries?
1 Unloading oxygen hb and diffusion into plasma
2 Loading and carriage of CO2 as bic and carbamino
3 exchange hco3 - and Cl- cross membrane - hamburger
cl bic tports band 3 protein capnophorin
Draw out from page 128 gas exhcnage in red cells
Oxygen unloading assists w/ co2 loading - Haldane
Co2 dix loading assists oxygen unloading from Hb bohr
What is haldane affect
Diagram
Increased ability o blood carry Co2 when Hb gives up O2
Art blood cotrain 48mls co2 and pco2 40
mix ven conitrains 52 at pco2 46
seen diagram - if position co2 dissoc curve not change when sat drop mix venous pco2 would rise to 55mmhg if same amount co2 carried
What factors are responsible for haldane effect
1 deoxy is 3.5 effective then oxy forming carbamino compounds - major factor accounts 70% haldane effect
Deoxy hb is better buffer than oxy mops up more H+ produced when h2co3 dissoc improve carriage CO2 as bic accounts remaining 30% haldane
Does formation carbamino compound by deoxy hb account any increased buffering capcity of deoxy
No pka of carbinmo - so low fully dissoc plasma ph - net increase H+ conc
rather increasing buffering
more H requiring buffering produced
What groups Hb accoutn buffer capacity at phys ph
imidazole groups pka 6.8
in 38 histidine residue in Hb
Differences between base & apex of lung
Top larger at end expiration lower ventilation lower perfusion higher v/q (3.3 vs .63 in base)
Higher vq - diffrence gas compositon
higher Po2
Lower pco2 higher ph
difference oxygen uptake and Co2 output
higher exp exchange ratio at apex vs base RER 2 v .67