Oxygen Hemoglobin Dissociation Curve Explained Clearly (Oxyhemoglobin Curve)

By Adem Lewis / in , , , , , , , , , , , , , , , , , , , , , , , , , , , , /

well welcome to another MedCram lecture
we’re going to talk about the effect of different things on the oxygen
hemoglobin dissociation curve okay so we’ve got a red blood cell from end on
kind of also looks like that with a little bit of a bulge in the middle and
that’s because it’s lost its nucleus what this is you have to remember is
simply a bag of hemoglobin it’s got no nucleus it’s got no mitochondria so the
only form of energy that it can do is glycol Isis or glycolysis and remember
that’s where we get glucose and it goes to basically goes to pyruvate and that
gives off forms of ATP this is not oxidative phosphorylation this is
substrate level phosphorylation but it gives the cell the ATP that it needs and
that’s important because there’s an intermediate in this glycolysis that’s
actually going to do something story hemoglobin binding curve which we’re
going to talk about next but before we get to that I wanted to explain to you
what the hemoglobin molecule looks like if you can kind of imagine it’s four
different subunits that are connected to each other okay and usually there’s two
alphas and two betas but that’s not important right now
so there’s for binding spots for oxygen to bind to so if it binds to the first
spot what happens is it causes a conformational shift with the next one
that causes oxygen to bind more affinity and that causes a conformational shift
with the next one which causes the oxygen to bind even more affinity and
finally that causes a conformational shift that causes the last one to bind
with even more affinity and so what happens is you get something called
cooperativity the other turn that they like to use in
biochemistry is called allosteric interaction in this case it’s not
allosteric inhibition because it’s actually making these globin molecules
more apt to bind the oxygen molecule the other thing that you might want to be
aware of is sometimes they have different terms for these hemoglobin sub
units if they are not bound to oxygen they’re known as the tense form or T and
if they get bound to oxygen then they’re known as R or the relaxed form the other
thing that happens that you may want to know is that when an oxygen binds to
this hemoglobin molecule a little carbon dioxide molecule comes off a little co2
and you should probably know that that’s known as the Haldane effect just some
trivia there so that when oxygen binds to hemoglobin it releases co2 and if you
see the co2 go up a little bit that’s known as the Haldane effect but let’s
talk about the human lobe and binding curve so the way that this is
represented we’ve kind of talked about this before in the other lecture on
delivery of oxygen is there’s a relationship between the partial
pressure of oxygen in the blood and the saturation of the humic loeben molecule
so this is saturation here and this is PA o2 and we can take that all the way
up to a hundred so this is a hundred this would be 50 this would be twenty
five seventy five this is the po2 what we’re talking about here and up to about
eighty we’re starting to see here that there’s a kind of a curviness
to this hemoglobin binding curve and so the key points here that I want to show
you is that there’s this sort of a plateau area here where increasing
levels of po2 will not yield much more in terms of the saturation so there’s
kind of a diminishing marginal utility in sociated with that the other thing I
want you to sort of notice is that if we were to shift this human blown
hemoglobin binding curve to the right in other
words if it were to go from this point to this point notice that in fact what
you’re seeing here is you’re seeing the hemoglobin molecule as a whole being
more apt to release oxygen it’s more apt to release oxygen and why is that
because at any given po2 let’s say 50 in this case you’ll see that in the blue
hemoglobin binding curve has a lower saturation then the yellow hemoglobin
binding curve and so therefore the blue hemoglobin binding curve is more apt to
be less saturated at a given po2 than the yellow hemoglobin binding curve and
that’s important because what’s actually happening as this thing is shifting back
and forth as it goes through the bloodstream depending on where it is so
this is kind of something that you should know so here’s a question what
are some things that are going to shift the hemoglobin binding curve to the
right and remember these are things that make it less affinity so the things that
make the hemoglobin binding curve less affinity to oxygen or all of the things
that you would expect to find in the blood where oxygen needs to be given off
by the hemoglobin molecule and that would be in the muscles or placenta and
what are they what do you find in the muscles are you going to see a high or a
low pH you’re going to see a low pH because this is where lactic acid is
being produced this is where carbon dioxide is being given off and we know
that carbon dioxide is a Lewis acid number two we would see a high
temperature okay your muscles are hot right when they’re working so that would
shift it to the right we already said that a high partial pressure of carbon
dioxide is going to shift the hemoglobin binding curve to the right
another thing that shifts it to the right is a molecule called D
e P G die phosphoglycerate otherwise known as to 3b PG or bisphosphoglycerate
this as you may recall is an intermediate of glycolysis and this is
where 3-phosphoglycerate goes to to phosphoglycerate and that’s
an important step in glycolysis because as that happens and as you have this
buildup of 2 3 BPG which is by the way seen elevated in pregnancy which makes
sense because in pregnancy you’re going to want your hemoglobin molecule to be
able to give up more oxygen to the fetus you’re going to do that you’re going to
see this increased in pregnancy and you’re going to see your hemoglobin
molecule giving up more oxygen to the fetus and you’re going to see this
hemoglobin molecule shift to the right okay now what are some things that you
would see cause it to shift to the left these are things that you would see in
the lungs so for instance in the lungs you’re breathing off carbon dioxide you
could have a low acidity so you’re going to have a high pH of course in the lungs
you’re breathing in air which is cooler than body temperature so generally
speaking you’re going to have a low temperature number 3 as we already
mentioned we’re going to have a low partial pressure of carbon dioxide and
of course 4 we’re not going to see maybe possibly as much DPG and so you’re going
to see a shift to the left the other thing that’ll shift it to the
left is fetal hemoglobin so H not a but actually F which is way out here ok and
that’s fetal hemoglobin sucks up that oxygen like no other human globin as it
comes by the placenta so that is the hemoglobin molecule and the
disassociation curve thanks for joining us
you you

100 thoughts on “Oxygen Hemoglobin Dissociation Curve Explained Clearly (Oxyhemoglobin Curve)

  1. CO2 isn't bound to the haemoglobin which is what it sort of sounds like, in the haldene effect the oxygenated haemoglbin molecule makes the blood more acidic, forcing dissolved co2 out of the blood

  2. See the whole series at www.medcram.com along with other top quality videos including reviews in pulmonary, cardiology, infectious disease, and hematology!

  3. Thanks! I had forgotten the small details from undergrad, I also didn't feel like getting up to get my Biochem book.

  4. Simply wonderful! I was struggling with this concept for days but
    understood it in less than 8 minutes after watching this video, thank

  5. Just found this channel while studying for a biochem exam… very helpful I was able to follow along with my note and this video just made things a little bit clearer for me!

    I couldn't study this curve for weeks and now that I'm cramming for my exam, this lecture helped a lot. Especially when I saw how the curve is drawn and which side is which with the factors affecting it.
    Thank you so much!

  7. He lost me at 4:37.

    "More apt to release oxygen" (curve moves to right)?? The x-axis is pressure (or partial pressure). That's pressure of what? The amount of pressure that oxygen is pushing back on the blood? So a full red blood cell, with 4 oxygens attached, exerts more pressure on its surrounding blood? What does that mean?

    Take for example, P50 (pressure of 50mm Hg)… at the same point, the yellow curve is higher. So the yellow curve has a higher saturation point, or more oxygens are in the hemoglobin carriers but exerting the same amount of pressure than the blue. So how does that relate to "how apt" it is to release, or not to release, oxygen?

    Totally confused.

  8. i have a question… In COPD exacerbation I have read that we should not give high levels of O2 as it may cause vasodilation to all parts of the lung >>causing shunting of blood but also "high level of O2 reduce the uptake of CO2 from the tissue via haldane effect" How does that make sense …i thought with more 02 you have an opportunity to unload more O2 to the tissue and pick up CO2 as well.

  9. awesome video. use it all the time to refresh. quick question. had it come up in work. what type of shift would hypemic hypoxia cause? I would assume a right shift to ensure perfusion. thank you in advance. your thought is much appreciated.

  10. Ive reviewed this concept every few years and its never stuck, but I think it will now–the way you tied in the muscles and lungs to the features that cause the curve to shift was extremely effective! Thank you for sharing!

  11. Man! I’ve been struggling to understand that curve until I reached this video, it really helped me. Thank you very much.

  12. o my! thank you. this makes so much sense than the text! i read the thing for like 20 times.. and everything got so much clearer after watching this.

  13. Can someone answer a question for me that has bugged me for a few days now? If you have a low haemoglobin (i.e. you are anaemic), will this impact upon the measurement picked up by a peripheral saturation probe? I believed that even if your haemoglobin levels have dropped, your saturations would remain the same, so long as all other physiological parameters remain the same. Is this true?

  14. I think u got the T and R form of Hb wrong. When the globin is bound to O2, its called Tensed state and when it isnt bound to the O2, its in relaxed state and has more affinity for 02

    please correct me if i am wrong …

  15. you said R state has less affinity of oxygen but doesn't it have a higher affinity? it is able to bind to oxygen, which causes the conformational changes within the hemoglobin transitioning it from the t state to the r state

  16. I'll bet he was starving, too.
    Have you asked the bald guy with the lizard-daggard stare thing going on?

    He has a Mini-Gun that pops out of his head when he needs it.
    (Usually Miss-Fires, but wow, the RATE!)

  17. Increases in fetal hemoglobin (FHb) will actually shift the curve to the right. The fetus steals the mother's oxygen with fetal hemoglobin and this decreases her oxygen saturation.

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