DIP Episode 409 - The Clutch Hemoglobin Podcast (for Step 1-3)

Okay welcome everyone my name is divine this is episode 409 of the divine intervention podcasts. And to this podcast we're gonna be discussing hemoglobin. This is gonna be the clutch hemoglobin podcast, the clutch hemoglobin podcast. If you know what's this cost here, that would be surprised if you get any hemoglobin related questions wrong on your exam. So obviously this is a podcast I'll be useful for people taking the USM list that wants to stick three exam. Now we all know that hemoglobin is the primary molecule that carries oxygen around in the blood, right? It's the thing that basically it's main primary job is that it's an oxygen carrier. It can carry other things or primarily worried about it from the perspective that it's an oxygen carrier. Although like I said, it can carry other things like carbon dioxide. And it carries carbon dioxide that's also known as carbamino hemoglobin carbamino C-E-R-B-A-M-I-N-O hemoglobin carbamino hemoglobin. Now hemoglobin remember is made of him and four globin chains. Those four globin chains essentially define the different kinds of hemoglobin that you can find in blood. So for example we have hemoglobin A that's adult hemoglobin remember it contains two alphas and two bitters. We have hemoglobin F that's the phytohemoglobin that contains two alphas and two gammas. Phytohemoglobin we know that we find it when you're in utero and it lasts about six months after you've been born.

That's why people with sickle cell disease and with many hemoglobinopathies don't have many problems especially if you have like beta thalacemia or whatever. You won't have significant problems for about the first six months of life roughly because that hemoglobin F is weird enough. But once that hemoglobin F wears off the person's problems will begin and we know that there's the drug known as hydroxyurea that inhibits ribonucleothyl reductase that is used as to raise your levels of phytohemoglobin. Now remember there is also hemoglobin E2 that's alpha 2 delta 2. For me we find it in most normal people. I believe you start making it pretty late in gestation for the fetus. But the thing is it can go up over normal when you have beta thalacemia. Especially beta thalacemia minor. But also you find it in beta thalmaid. Really any beta thalacemia will be associated with an increase in hemoglobin E2. So if you see an increase in hemoglobin E2 in your USML exams you want to think about beta thalacemia. Because again hemoglobin E2 is alpha 2 delta 2. So it doesn't need beta globin chains. So if you have a beta globin chain deficiency you're going to make more of the hemoglobin that do not involve beta chains like hemoglobin E2. And then there is hemoglobin H. Remember hemoglobin H is the one that is found in certain kinds of alpha, not beta alpha thalacemias. Beta globin H is when you have the beta globin chain from an attachomer. So you bring four beta globin chains together.

Those people tend to be very transfusion dependent. But those people are born alive. They don't die in the year. Because remember in alpha thalacemia there are four alpha globin chains that people have. If you're missing one or two that's not ideal. But most of those people either have no symptoms or they have a mild anemia. But if you lose three of the four you're going to have what we call hemoglobin H disease. If you're hemoglobin H disease you have four beta's coming together. And then the worst kind of alpha thalacemia is where you have all four genes lost. So you literally have no alpha. You can already be interested that those people have problems from being evenly uter. Because in uterol you need hemoglobin F as alpha 2 gamma 2. If you have no alpha chains then those gammas, the only logical thing that makes sense is that they will all come together and form a gamma tetramer. That's what's called hemoglobin BART. Those kids do not get born alive. Those kids are born still born. That's pretty high you to know. So if you see a child that doesn't make it to term is not born alive and his alpha thalacemia is going to be hemoglobin BART that they have. And then the other two hemoglobin that I will say are pretty high you to know are hemoglobin S which we find in people with sickle cell disease. And the hemoglobin C. It's actually another variant of sickle cell disease, but it's another hemoglobin variant that can be found in certain people.

Remember hemoglobin S, the problem there and these two disorders hemoglobin S, hemoglobin C. The problem is with the beta globin chain. These are not alpha globin chain problems. They are beta globin chain problems. Now in hemoglobin S, the glutamic acid that is on the beta globin chain is substituted for valine. That's very high you to know. When hemoglobin C, the glutamic acid that is on the beta globin chain is substituted for lysine. Right. So valine for sickle cell disease, lysine for hemoglobin C disease. So, I know some people may be like, devine how do I remember this? Just remember that glutamic acid is changed in either case and then just go in alphabetical order. Hemoglobin C. C comes before S, that's hemoglobin S in the alphabet. Lysine L comes before V in V in the alphabet. If you keep those rules in mind, you're going to be pretty set from that perspective. So make sure you understand these different hemoglobin. It's kind of important. And the thing with hemoglobin is that hemoglobin contains iron. It can contain iron in the 2 plus 4, that's feroz iron. But it can also contain iron in the 3 plus 4, that's feryc iron. The feryc iron has a 3 plus hemoglobin, cannot carry oxygen. The feroz 1, that's a V2 plus, can carry oxygen. In fact, whenever you have hemoglobin, that contains iron in the 3 plus 4, that's what's known as methemoglobinemia. Remember that that's a problem you get into when you take a very powerful oxidizing agent.

Especially these local anesthetics that end in the cane, like benzocaine, for example. Or certain medications like sulphur drugs, nitrates, those things can induce a methemoglobinemia. As we know, the way you fix methemoglobinemia is by getting that feryc 3 plus iron back to the feryc 2 plus 4, that can carry oxygen. We do that with methylene blue, we do that with methylene blue. And if you don't see that as an answer on the exam, you can consider vitamin C. Vitamin C also catalyzes or speeds up the conversion of feryc 3 plus 2 plus. It's just not as efficacious at that process as methylene blue. That's something I definitely want to know, for example. And remember that when you have problems with hemoglobin, because remember I say that hemoglobin contains heat and globin. So the hem part, remember, can be synthesized. So we've been talking about all these globin problems, globin problems, globin problems. But there are hem, there is hem-related issues. There's hem-related issues. Remember the hem-related issues are the porphyrys. Because remember first things first, to synthesize hem, the relative enzyme is amino level lenec acid synthetase. In the synthesis of hem, you can get into certain problems. You can have deficiency of porphyrylinoge in the amines, right? Pino porangeli diaminase. That's what we call acute intramethanpoferia. It has a lot of more dominant inheritance.

And typically it's going to be in a person that has neuropsychic synthomes, abdominal pain, and dark collodury. Neuropsychic synthomes, abdominal pain, dark collodury, that's the classic presentation on exams. And you know, if those toxic things accumulate, that's usually problematic. So typically in those people, the way we treat them is we give them something that will inhibit alas, that's the retinutinance of hem synthesis, amino level lenec acid synthetase. If you inhibit alas, then those nasty things will not build up. When they don't build up, then you won't get in trouble. So you can do that with IV glucose or IV heme or IV heme tin. Those are all high offense to know, right? And then don't forget porphyrytinotardar. That's a Euro deficiency. Euro is Euro porphyrynogen. Euro porphyrynogen decarboxylase. Euro porphyrynogen is spelled UROPORPORPHY. So porphyrynogen, PHY, RIN, OGE, decarboxylase is DE-C-A-R-B-O-X-Y-L-A-S-E. Euro porphyrynogen decarboxylase or UROD for short. That one is not, don't think of it as a heritage but a sort. So I'm not going to say all of those on my lenithen or x-linked lenithen. Think of it as more of a spontaneous tinnularisis. It has a special, strong association with hip-c infection. That's a pretty high-yield association to know. And porphyrytinotardar, those who are going to have skin problems, right? Look at the name, porphyrytinotardar. They won't have neuropsych symptoms.

When you see some hip-c going on, you may see some skin issues going on. You may see hypertrophicosis. They'll have a lot of hair. When you see the think of porphyrytinotardar, that's for the olflobottomine. And those people, if a person is diagnosed with porphyrytinotardar, your next step in management is to check their hip-c status. Check their hip-c status. That's pretty high-yield to know. And if they have one that's lying in hip-c, you can treat that hip-c. Remember hip-c, you can treat it with interferon alpha. But you can also use those direct-acting antivirals, like sofosbovir, le de pa-svir, things like that. Those NS protein inhibitors. That's pretty high-yield to know. So overall, you can treat porphyrytinotardar with flobotomy. So don't forget your porphyrytinotardar with flobotomy. So don't forget your porphyrytinotardar with flobotomy. Those are the big things to keep in mind. Remember, lead also messes up that hym synthesis pathway. That's why lead can cause a micrositic anemia. Whenever you mess up hym synthesis, that can cause micrositic anemia. So lead inhibits a lot, early dehydrates, and also inhibits ferrokylates. When inhibiting those enzymes, you're not going to be able to make hym properly. You're going to have a micrositic anemia. And addition to the peripheral neuropathy, like wrist drop, foot drop. You can see those lead lines, especially in the bone. You can actually see those things pretty well on an x-ray. Because remember, lead is a metal.

So it's going to light up. It's going to read your dance. You're going to find it on an x-ray. So these are all things you want to keep in mind for, for example. These are all things you want to keep in mind for exams. And then don't forget, you know, hym synthesis, right? hym synthesis is pretty important, right? Hym synthesis is one of the wisdom diagnosed diabetes. If you're A1 C is over 6.5%, 6.5% to diagnosed with diabetes. Although remember, the A1 C is not particularly useful in people that have chronic amolases. If you're the kind of person that has chronic amolases, then A1 C is not helpful. Because the red blood cells don't live for as long as they should. So if you measure the A1 C in those people, you may be getting a falsely depressed, A1 C level. You may say that they don't have diabetes when they, in fact, do. So you'll be missing out on a lot of people that have diabetes. So A1 C is not particularly sensitive for the diagnosis of diabetes in people that have chronic amolases. They can literally make a biostatistics question out of that, okay? So A1 C has low sensitivity in people that have chronic amolases. Why does they have low sensitivity? Because again, it's going to be missing out on people that have disease. When we're dealing with people that have disease, we're talking about sensitivity, right? That's a biostatistics question right there.

And just as a quick segue before I jump to the second half of our discussion today, if you're taking your USML-1 STEP2 CK or STEP3, or complex level 2 or 3 exams, anytime soon, I have three courses that you may find to be helpful. Especially if you want your scores back in time, especially from the USML perspective, before ERA's applications are downloadable by programs. I have first an MBA me testing and strategy scores. This for STEP2 and STEP3 is going to be taking place on the 17th of August. That's a Wednesday. That's next Wednesday from 4 to 6.30 pm, Pacific Standard Time. Many people have taken these courses. They found it to be profoundly helpful. We really address how to tackle MBA me exams as a test. Because sometimes you see some people, they have the knowledge, but they're just bad at taking tests. If you come to that class, you'll learn how to take not just any tests, but the MBA me tests. It's very useful for anyone taking shelf exams, anyone taking step 2 or step 3. And then I have a 20 hour review course. It's going to be taking place from the 25th to the 26th of August. It's 20 hours, 10 hours each day. We'll meet from 7 to noon, from 1 to 5, 1 to 6 pm, Pacific Standard Time, on each of those two days. Again, I strongly suspect that you'll find those courses to be helpful. Again, we're going to discuss internal medicine, pediatrics, oligone, psych, surgery, bio stats, ethics, multi-systems, processes, and disorders.

We've done this course a lot of things, healthcare systems, communications. Again, many people have taken these courses, they've done really well. I get emails from people very regularly. Like I got a lot of emails yesterday from people that took the course, the last courses that I held. At least over the last few weeks, and they go their scores, they pass, they get really well. So the 20 hour course is targeted to a complex level, 2 and 3, and step 2, see, can step 3. And really, to be honest with you, if you're a person that is just studying off your 30 year of med school, and you're like, I want a good overall review of everything. Like the key things to take away, exam wise from most of the rotations I'm going to be doing, it's a fantastic course for you to take. Or if you're a midway through your 30 year, you're like, I want to review many things. Because again, the course, I don't just give you information. I try to help you integrate, and I try to make sure I explain, within reason, you can explain pathophysiology for every single thing. But within reason, I try to explain pathophysiology. So it's something you find to be super, super helpful. And obviously, it's also intended, but we will take in the step 2, see, exams and step 3. And then I have a value statistics bootcamp. That's the final course I offer. It's going to be taking place on the 18th of August, that's next week, Thursday, from 5 to 9 pm, Pacific Standard Time.

That's intended for anyone taking step 1, step 2, see, or step 3. The thing is, many people studying for these exams, I think you're realizing that most of the Indian equations, these, these are not plug and chalk. They are not. Most of them demand understanding. Many times you don't actually have to do math to solve most bio-stats questions. But many resources for bio statistics, they just focus on the formulas, and that's not the substance of bio-stats. The substance of bio-statistics is understanding. So if you want to gain that understanding, attend the bootcamp, it's 4 hours, it's going to be really this course and all the other courses over Zoom. You'll see who do some math, but a lot of it is just getting your reasoning down for 4 hours, you'll see bio statistics from many different angles. I will talk about research studies and tests, bio statistical tests and all those, all those things. But let's go on. So if you're interested in any of these things, just shake me an email through the website, and I'll give you some more information. So now let's continue on discussion of hemoglobin, right? So we've talked about the different types of hemoglobin and what not, right? So don't forget, right? That hemoglobin, you know, like I said, the normal adult hemoglobin, hemoglobin A, alpha 2 beta 2. That those beta globin chains, we have the ability to bind 2, 3 BPG. Remember 2, 3 BPG is one of these split of products from glycolysis.

It's one of these split of products from glycolysis. 2, 3 BPG is actually made from 1, 3 BPG. It's made by BPG mutates. So it literally mutates. It's not mutates, but that's aware. Remember, convert 1, 3 BPG. You're literally rearranging molecules, right? From 1, 3 to 2, 3. So 2, 3 BPG binds to the beta globin chain, right? And it basically causes it to release oxygen. And one thing that's pretty helpful to understand is if you know that 2, 3 BPG binds specifically to the beta globin chain. And that tells you that phyrohemoglobin must not be able to bind 2, 3 BPG. Because remember, phyrohemoglobin is alpha 2, gamma 2. So since it has no beta globin chains, it cannot bind 2, 3 BPG. So since it cannot bind 2, 3 BPG, phyrohemoglobin, it has a much higher affinity for oxygen, which is advantageous. Because in uiterone, you want to be collecting oxygen from mom. So to collect that oxygen from mom, you need to have hemoglobin that has a higher affinity for oxygen. And the hemoglobin that we'll find in mom, mom has hemoglobin A. Ud the phyros, you have hemoglobin F. Mom, alpha 2 beta 2, Ud phyros alpha 2, gamma 2. So hemoglobin F actually has a left shifted, left shifted oxyhemoglobin saturation curve, left shifted. Because again, it has a higher affinity for oxygen compared to hemoglobin A. Okay? Hemoglobin F has a left shifted oxyhemoglobin dissociation curve. And remember, you know, BB gets oxygen from mom. You know, if I have the umbilical veins, right through the placenta.

And remember, the umbilical arteries bring more of the tick, more of like the oxygen ether blood. Okay. So again, don't forget, hemoglobin is a multi-subunit protein, right? It's a multi-subunit protein. So because it's a multi-subunit protein, you know, it presents a lot of opportunities for a lot of other allosteric molecules to bind. They combine to specific sites on hemoglobin. And really the binding of these molecules, you know, again, pretty much like any other allosteric molecule, it's going to modulate the affinity of hemoglobin for, for its substrate, right? And what we're doing is, you know, the binding of the oxygen is a lot of oxygen. And so, the binding of the oxygen is a lot of oxygen. And so, the binding of the oxygen is a lot of oxygen. And so, the binding of the oxygen is a lot of oxygen. And so, the binding of the oxygen is a lot of oxygen. And so, the binding of the oxygen is a lot of oxygen. And so, the binding of oxygen is a lot of oxygen. And so, the binding of oxygen is a lot of oxygen. And so, the binding of oxygen is a lot of oxygen. And so, the binding of the oxygen molecules, that's what's known as positive cooperativity. That's essentially what is responsible for the S shape of the oxygen-hymoglobin dissociation curve. That is literally what is responsible for the S shape of the oxygen-hymoglobin dissociation curve. That's why it has that S shape because of positive cooperativity. Now, the thing is, the oxygen-hymoglobin dissociation curve, right?

There are certain things that can cause it to shift right. When it shifts right, it means more oxygen is being released to tissues. It means your hemoglobin is having less affinity for that oxygen. So, it's being released into tissues. So, what are some of those conditions that can cause that? Well, low-peach conditions, right? So, if you have like increased hydrogen ions, or if you have increased CO2, because remember CO2 would dissolve in water and they convert it to carbonic acid and then carbonic and hydrogen would do its thing and convert it to bicarbonate hydrogen ions. So, those hydrogen ions are going to shift the shift things right. And then also, if you increase the temperature, increase temperature, if you go to a higher altitude, because think about it, right? When you go to a higher altitude, there's less oxygen in the atmosphere. The percent is the same, but that, you have a percent of a smaller pi, right? Because as my first atmospheric pressure goes down as you go higher, right? So, that's, you're going to need more oxygen release, right? So, in those situations, you're going to have a right-shifted curve and also the presence of 2, 3, b, b, g, right? And then, those things all cause, all, he'll be able to have decreased oxygen affinity, right? So, you're going to release more oxygen to tissues, right?

And really, one of the easiest ways to, because many people just memorize less of stuff, one of the easiest ways to memorize these parameters is just to think in terms of the exercising individual. The person that's exercising is going to have many of these things I'm seeing as your exercise, you're making a lactic acid, right? That's a low pH condition. You're generating a lot more CO2, right? And then, you're going to have more CO2, right? And then, you're going to have more CO2, right? And then, you're going to have more CO2, right? And then, you're going to have more CO2, right? And then, you're going to have more CO2, right? And then, you're going to have more CO2, right? And then, you're going to have more CO2, right? And then, you're going to have more CO2, right? And then, you're going to have more CO2, right? And then, you're going to have more CO2, right? And then, you're going to have more CO2, right? And then, you're going to have more CO2, right? And then, you're going to have more CO2, right? And then, you're going to have more CO2, right? And then, you're going to have more CO2, right? And then, you're going to have more CO2, right? And then, you're going to have more CO2, right? And then, you're going to have more CO2, right? And then, you're going to have more CO2, right? And then, you're going to have more CO2, right? And then, you're going to have more CO2, right? And then, you're going to have more CO2, right?

And then, you're going to have more CO2, right? And then, you're going to have more CO2, right? And then, you're going to have more CO2, right? And then, you're going to have more CO2, right? And then, you're going to have more CO2, right? And then, you're going to have more CO2, right? With more affinity, 244 more affinity. And then, when carbon monoxide is bound to hemoglobin, and we call it carboxy-hymoglobin. Remember, carboxy-hymoglobin is hemoglobin bound to carbon monoxide. Carbaminohymoglobin is hemoglobin bound to carbon dioxide. So, the thing is, carbon monoxide, you know, is binding to the Fe2 plus ions in hemoglobin. Then, oxygen cannot bind. So, that's the first problem you face. So, your SAO2 goes down. But, that oxygen that is already there, the second we heard to is the oxygen that's already on the hemoglobin. Before the carbon monoxide binds, it's more difficult to release. So, carbon monoxide poison actually causes a left shifted oxy-hymoglobin curve. It causes a left shifted oxy-hymoglobin curve. Since it's left shifted, you're going to be less likely to release oxygen to your tissues. So, you're going to run into problems. Now, the reduced number of binding sites for oxygen on that hemoglobin as well. In carbon monoxide poisoning, it's also going to cause a downward shift in your oxy-hymoglobin curve. I'm seeing this more in pretty much the choir that's going to be taking step one.

Carbon monoxide poisoning causes a left and a downward shift of your oxy-hymoglobin curve. Because, if you think about it, when carbon monoxide is bound to hemoglobin, an oxygen cannot bind. You've literally reduced the capacity of hemoglobin as a protein to carry oxygen. If you essentially decrease the V-max, it's causing a downward shift. It's causing a downward shift. It's causing a downward shift. So, again, it can discuss this literally in Nicholas' mentee terms. That's why you want to be able to think about things in a multi-dimensional fashion, one example. It causes a downward shift, essentially killing your V-max. Don't forget, carbon monoxide. Hemoglobin has 244 more affinity for carbon monoxide than oxygen. We think about carbon monoxide poisoning on your exam. When you mention a personal chair, a lip or a person in a house fire, who presents the emergency room with a headache. Your treatment is high-floor oxygen or hyperbaric oxygen. High-floor oxygen does a pretty good job. Hyperbaric oxygen is better. It's not every hospital that has access to hyperbaric oxygen. So, please don't forget, when you have carbon monoxide poisoning, your blood oxygen saturation, your p-lidu-eo-2 is normal. It doesn't affect any binding of oxygen to your actual blood. Oxygen dissolved in blood. It's the oxygen bound to hemoglobin that suffers. So, your p-lidu-eo-2 is normal, but your s-lidu-eo-2 is decreased in carbon monoxide poisoning.

If you want more information on poisoning, actually have a podcast that I made earlier recently, a few weeks ago, on the three confusing Poisonins. Just do a Google search for it, the three confusing Poisonins. In that podcast, I'm pretty sure I compare carbon monoxide poisoning to cyanide poisoning, to methemoglobinemia. I talk about it at a much deeper level than I did in this podcast. So, you're a pretty high-yield podcast to know, because one of those things that pretty much show up on essentially all the USMID exams. Now, the final final thing I want to say here today, is that hemoglobin can exist in one of two forms, right? It's the top form, the TAUT form, that has a reduced affinity for oxygen. And then there's a relaxed form that has an increased affinity for oxygen. So, the top form, the T in top, is favored in tissues. Remember the T in top's T in tissues? It's helpful, right? Because you want hemoglobin that has low affinity for oxygen in your tissues. Because in your tissues, you want to be releasing that oxygen, and binding up that carbon dioxide. The relaxed form is favored in the lungs. In the lungs, that's where your hemoglobin literally picks up oxygen. That's where your hemoglobin literally picks up oxygen. So, you want that form to be favored in the lungs, because in the lungs, you literally pick it up oxygen. And again, the things I said earlier that cause a left shift. I mean, a right shift of the oxygen-emoglobin saturation curve.

If you take the reversal, it's open, where is another list for the things that cause a left shift? Just literally take the reverse of all those things I mentioned. And then don't forget that hemoglobin F is also left shifted. And carbon monoxide poisoning also causes a left shift of your oxygen-emoglobin dissociation curve. So, that's something that's pretty, pretty high yield to know. And then I'm just imagining if the wearer was set up some question, where you see two left shift that oxygen-emoglobin saturation curves. And then they're trying to ask you which one represents carbon monoxide poisoning. And which one represents hemoglobin F? Hemoglobin F will be left shifted, but I imagine that it should not have a downward shift, because you shouldn't have like a lower V-max, right? You can still carry as much oxygen. You're just less likely to release it. But in carbon monoxide poisoning again, like I said, because it's a left shift, but it also causes a downward shift. You're literally crushing the V-max, because carbon monoxide when it sits on hemoglobin, the place is set, oxygen cannot sit anymore. So again, I really hope you'll find this podcast to be helpful. I think I'm going to go ahead and pause here. I'm going to offer one on one tutoring for all the USML exams, step one to three, all the complex exams, complex one to three. I also offer longitudinal tutoring.

If you're studying out in school, I can tutor you throughout your preclinical courses, which many times will set you up nicely for step one. I can tutor you all three or third year. If you're a third year med student, tutor you for that, tutor you for your shelf exams, and that will prepare you very strongly for step two. And then I also offer review courses for biostatistics, for step two CK, and step three, complex level two and three. And I also offer an MBA meetistic and strategy scores. And then I have these podcasts on Divine Intervention Podcasts.com, everything from episode one to four zero nine. If you actually have a Word Press account and you subscribe, you will get an email notification whenever I make a new podcast. And then I also have these podcasts on Apple podcasts, on Google podcasts and on Spotify, at least the most recent 150. It's a rule. I can't put more than 150 on there. The most recent 150. If you want everything from episode one, just go ahead and check out the website. Then I have a You Tube channel, Divine Intervention, USM Li Podcasts and videos, Divine Intervention, USM Li Podcasts and videos. That's literally where I post the videos that I make. And I also make, you know, purely copies to the You Tube channel. Just go ahead and hit subscribe, every little bit of support certainly helps. And then finally, my new website is called our Divine Intervention Life Lessons.com. Many of you that listen to this podcast know I'm a Christian.

So many people have said, wow, Divine, I love your life lessons. Oh, that you put at the end of your podcast. So I says that a new website. I'm still going to be seeing some life lessons here and there here. But go to Divine Intervention Life Lessons.com. I make two podcasts every week. They will tend to 20 minutes long. I just got a life lesson from a biblical perspective. Again, many people have actually emailed me from that and said, well, I found it to be really helpful. And I have a podcast associated with that. It's on Apple podcasts. It's called the Divine Intervention Life Lessons podcast. And then finally, we know that era season is upon us. If you need help with your era's applications, recommendation letters, personal statements, the supplemental application, your era's application itself, more interviews, worked with tons of people in that regard. If you're interested, just shoot me an email. And I'll give you some more information. So thank you for listening to me. Have a wonderful Thursday. I'll see you next time. God bless you. Thank you.

To carry oxygen in the blood.

Hemoglobin F ($\text{HbF}$).

Because it has a higher affinity for oxygen, which is advantageous for collecting oxygen from the mother in utero.

Neuropsychiatric symptoms, abdominal pain, and dark urine.

Glutamic acid is substituted for valine on the beta globin chain.

Methylene blue (or Vitamin C, which is less efficacious).

In association with beta-thalassemia.

$\text{Hb Bart}$ ($\gamma_4$). These individuals do not survive to term (stillborn).

Hemoglobin H disease.

$\text{Hb S}$: Glu $\to$ Val (Valine). $\text{Hb C}$: Glu $\to$ Lys (Lysine). Remember alphabetical order: C comes before S; L (Lys) comes before V (Val).

It causes both a left shift (high affinity) and a downward shift (decreased Vmax/reduced capacity).

Defect in porphobilinogen deaminase.

Low sensitivity, because red blood cells do not live long enough to accurately reflect average glucose levels.

$\text{Hb Bart}$ ($\gamma_4$). These individuals do not survive to term (stillborn).

Hemoglobin H disease.

$\text{Hb S}$: Glu $\to$ Val (Valine). $\text{Hb C}$: Glu $\to$ Lys (Lysine). Remember alphabetical order: C comes before S; L (Lys) comes before V (Val).

It causes both a left shift (high affinity) and a downward shift (decreased Vmax/reduced capacity).

Defect in porphobilinogen deaminase.

Low sensitivity, because red blood cells do not live long enough to accurately reflect average glucose levels.