We said that a protein is a three-dimensional coiled up chain of amino acids that are arranged in a precise sequence. And they really do kind of look like slinkies. The chain of amino acids themselves is called a polypeptide chain and once it takes on a three-dimensional shape, it's referred to as a protein. It's only as a protein, coiled up as a protein, that it's functional. cause the protein to uncoil back into a straight polypeptide chain.
We call that denaturation. It's become denatured. It no longer works. And we identified three things that would cause proteins to become denatured. What were they?
They're listed right here. High temperature, hyperthermia, acidosis or alkalosis, or exposure to certain heavy metals. And we talked about each one of those.
All right. We then started reviewing... amino acids, the structure of an amino acid.
And it begins with a carbon atom. We know every carbon atom forms four covalent chemical bonds. Attached on one side is an amino group. On the other side, we'll call it an acid group, technically known as a carboxylic acid group. Here in this bottom position is a hydrogen atom.
And up on top is the rest of the molecule. And it might be just a hydrogen. It might be an OH.
It might be something more carbon. complex. There are 20 different types of amino acids based upon what's attached in this R position.
And we actually looked at that briefly last time, last week, on page A14. So on A14, in the lower half of the page, we saw five different amino acids, glycine, leucine, phenylalanine, lysine, and cysteine. And we learned from that, first of all, that most amino acids have the ending E.
There's always exception to any of these patterns. patterns, but in general that's the pattern. You'll notice that glycine just has a hydrogen, it's the simplest of all the amino acids.
In contrast, phenylalanine has a benzene ring, it's a ring structure, it's more complex. And, all right, so those are amino acids. Now, one other thing before I go any further, let's jump to page A16.
We may have looked at this last time. I can't remember. On A16, how are amino acids snapped together?
What do we call the chemical reaction that allows amino acids to be joined together? a dehydration synthesis reaction. This is the common way that organic molecules are joined together. We have learned previously that that's the way sugars are snapped together.
That's the way fatty acids are attached to a glycerol to form a monodire triglyceride by a dehydration synthesis reaction. And that's the way amino acids are joined together. Conversely, if you had a polypeptide chain and you wanted to start breaking it apart in the individual amino acids. That would be called what kind of reaction? Hydrolysis.
A hydrolysis reaction where you have to add water in order to cause lysis, rupturing, breaking it apart. So I'm just reminding you of that. On page A15, on A15, you'd say what page are we? A15.
So this is a listing of all 20 types of amino acids, and we did say there are 20 different types. Now, we need all these amino acids in order to build, to construct the protein. in our body.
Just like, and here's an analogy I'm going to give, if you wanted to write sentences and you're typing on a keyboard, you would need all the keys, all the letters. in order to type a sentence. Now, that doesn't mean that every sentence you write contains all the letters of the alphabet.
For example, we don't have many words that use the letter X or Z. So it's very possible that you write sentences all the time and rarely ever use the letter X or Z. Similarly, not every protein contains all 20 amino acids. Alright? Some proteins might have all 26, I'm sorry, 20 amino acids.
It's 26 letters in the alphabet. Some sentences might contain all the 26 letters in the alphabet, but certainly most sentences don't contain all the letters and most proteins don't contain all the letters. All the amino acids.
Now, when we eat food, right, our food we know contains carbs and fats and proteins and nucleic acids. Those are the four major types of organic compounds that make up our food. So, when we eat proteins, we learned on page A3, when we were talking about the digestive system, that our digestive system digests or breaks apart carbs into monosaccharides.
And that's what we observe. absorb into our body. Lipids are broken apart into fatty acids and that's what's absorbed into our body. Proteins are broken apart into amino acids and that's what's absorbed into our body.
So that's how we get these amino acids. Now if we eat lots of different kinds of foods we'll get all 20 different types of amino acids. But any single food may not have high amounts of all 20 types of amino acids because we just said not all proteins can.
contain all 20 types of amino acids. So the proteins you're eating may not have all of these amino acids. Interestingly, of the 20 amino acids, approximately half of them, approximately 10, are regarded as non-essential and only the other approximately 10 are regarded as essential. Now you say, well wait a second, you just told us we need all the amino acids in order to build all the proteins that we manufacture in our body.
So how can... some be considered about half considered non-essential. So interestingly the cells of our body have the enzymatic machinery to convert these essential amino acids into these non-essential ones. So for example whether or not we get adequate amounts of tyrosine, this amino acid in our diet from the proteins in our food that we eat, even if we don't get adequate amounts of tyrosine.
Our body can convert this amino acid called phenylalanine into tyrosine. So we don't really need tyrosine. It's okay if we get it from the proteins we digest in our food, but even if we don't, we can make it from phenylalanine.
However, we can't go in the reverse direction. We cannot convert tyrosine into phenylalanine. So phenylalanine is an essential amino acid. We've got to get it sufficient amounts in a... of the proteins that we eat in our food or we're going to be in trouble because we won't have all the amino acids we need to build the proteins that are in our body.
Now some of you have had a nutrition class. Who's had a nutrition class? Anybody?
So if you had a nutrition class, they might have told you which food of all foods is considered the most ideal food as far as providing the best balance of essential amino acids. Anybody remember what that is? Which food?
It's actually advertised as nature's most perfect food. The incredible edible egg. Anybody ever hear of that? Eggs have an ideal balance of the essential amino acids. Now, most meat, most fish is also pretty good with all the essential amino acids.
However, plants, when you eat foods from plants, grains, vegetables, and fruit, they usually are lacking some of these essential amino acids. And that's why, is anybody a vegetarian in the class? vegan? Alright, most vegetarians or vegans know that because they're not eating eggs and meat and so on, which usually have a lot of these essential amino acids that we require, if they're eating vegetable matter, they know they must mix and match and combine different plant products to ensure that they're getting the essential amino acids that are required.
So in fact, beans, which are pretty good sources of protein, are nevertheless low in some of the amino acids. essential amino acids. But if you eat beans with, let's say, rice or corn, some of the amino acids that are missing in beans are found in rice or corn.
So if you mix them and match them, as it were, you get all the essential amino acids you require. I'm not going to get into all this stuff, but this is all kind of nutritional stuff. So they actually make a distinction in nutrition classes between those foods containing all the essential... amino acids that we need and those foods that don't they call them complete protein foods or incomplete protein foods i don't know if anybody remembers that from nutrition no not at all you don't certainly don't i mean if you'd like to i'll be happy to test you on it but i'm not asking you to memorize it i want you to understand what's meant by an essential amino acid It's meant by a non-essential.
And why is it non-essential? Again, to repeat, why it's non-essential is because we can convert this essential one into it. And that's true with all these.
We can use these to make these. Alright, so just understand that. Now, there are thousands of different types of proteins in our body and in every other living thing.
How do these thousands of different proteins differ from one another? They differ from one another in the way that they are called. one another in four ways. Number one, the proteins, thousands of different types of proteins differ in the number of amino acids making it up.
Some proteins might be 50 or 60 amino acids long and other proteins might be 400 or 600 amino acids long. Secondly, the proteins differ in the types of amino acids. As I mentioned earlier, some proteins might contain all 20 different. different types of amino acids. Other proteins might contain only 16 of the 20, 12 of the 20 amino acids.
Thirdly, they differ in the ordering of the amino acids. Even if we had two different proteins, two different proteins, they both contain all the amino acids, all 20 types, that doesn't mean those amino acids are arranged in the exact same sequence, the same order. And fourthly, The proteins differ in their three-dimensional structure and how they're coiled. And every single protein has different molecular configuration or shape as far as how it works.
So these are the four ways that the thousands of different proteins in our body or in chickens or in redwood trees differ from one another. Let's just remind you of some examples of proteins in us. And and other living things, but specifically us.
Arguably the most important proteins in any living thing, including us, are enzymes. And there are, each enzyme catalyzes a biochemical reaction. The word catalyze means it causes, it initiates, it activates a chemical reaction to occur.
Without enzymes, no chemical reactions would basically happen in our body. For every single chemical reaction, there's a different enzyme. Thank you. And if you think about it, you'd say, wow, there must be a lot of different chemical reactions occurring in our body.
You're right. And that's why there are thousands of different types of enzymes alone. Now, how do enzymes work? Enzymes attach to what is called a substrate or reactant.
And after they attach to the substrate or reactant, they cause a change in the substrate so that what is formed is known as the product. To help you visualize this, let's look on the next page, A16. So on page A16, Here it's showing an enzyme, protein. All proteins we said basically look like my slinky.
They're just coiled differently. And here it shows this enzyme attaching to a substrate, also known as a reactant. And in this picture it's a little bit more diagrammatic, not quite as realistic looking. But what does it show?
So it shows an enzyme that is named sucrase. And as you all know, enzymes usually are named with this suffix ending of"-ase". There are some exceptions. And so we take the ascending, that indicates an enzyme, and we name this enzyme based on the substrate that it attaches to.
So since this enzyme attaches to a substrate called sucrose. we call that enzyme sucrase. Anybody remember what sucrose is?
Table sugar, right? C and H sugar from Hawaii, right? Cane sugar. So sucrase attaches to sucrose.
That's the substrate. And then this enzyme, in this particular case, splits it. It splits it. Now, of course, in order to split it, it does also need, it also, it, it, it, it, it, it, it, it, it, it, needs water to split it.
It is a hydrolysis reaction. So let's just remind you, it is a hydrolysis reaction, and it's called hydrolysis because it needs H2O in order for this to work. But fundamentally, and then it causes lysis or splitting. And sucrose is split apart, forming glucose and fructose.
Those are the two monosaccharides that make up the disaccharide sucrose. These are the products. These are the products.
So in fact, sucrase is a digestive enzyme. It's an enzyme produced in our digestive tract. Every time you have C&H sugar from Hawaii and any food that you're eating... you have to split it apart into monosaccharides in order to absorb it. We only absorb monosaccharides.
Now, in this particular case, in this particular reaction, it's a reversible reaction. It can go in either direction. direction. Not all chemical reactions are reversible.
You learn in your chemistry classes and in biochemistry classes there are endergonic reactions and exergonic reactions, some need energy, some release energy. I'm not going to get into all that. But this particular reaction is reversible so that the very same enzyme that splits sucrose apart, that very same enzyme can actually join glucose and fructose together and and reform sucrose. We might ask then, well wait a second, if this very same enzyme can either cause this reaction to go this way or it can cause the reaction to go this way, what determines which direction the reaction goes in?. Basically, this follows what you learn about in a chemistry known as a mass action equilibrium.
You might remember those K equilibrium values. So it has to do, you remember, K equilibrium equals products over reactants. Remember that kind of thing?
So it just has to do with if you start with sucrose, the enzyme forms glucose and fructose. If you start with glucose and fructose, it drives the reaction to join them together to form sucrose. So the reaction always goes in the direction.
It's driven by what you start out with. What are your reactants? What are your substrate reactants that you start out with and the reaction is driven to form the opposite.
But again, chemical reactions can be more complex. All right, so much for an enzyme. Let's go to the previous page, again, A15. So we've talked about how an enzyme works.
Commonly, they will describe the way an enzyme attaches to a specific substrate or reactant. as very similar to the way a key fits into a specific lock. They'll call that a lock and key model. So I have a whole bunch of keys in my pocket here, and no matter how many keys you have, any given key will only open one particular lock.
So it's very specific. And similarly, each enzyme is very specific for activating a specific chemical reaction. Now, what are coenzymes?
So coenzymes is really vitamins and minerals. Largely, most vitamins and minerals function as coenzymes. Now, the way that I try to describe a coenzyme... is very much like a co-pilot. You say what do you mean?
Well many planes, some planes, little planes, these little planes are pretty simple to fly, not for me but for somebody who knows how to fly a plane. and all it takes is a pilot to fly these planes. Other planes are more complicated, and you not only need a pilot, but you've got to have a co-pilot, because one person alone cannot fly that plane.
Similarly with chemical reactions. Some chemical reactions are pretty simple, and all you need is the enzyme. Other chemical reactions are more complicated, and you need not only an enzyme, but even a coenzyme.
In fact, you might need several coenzymes. to make that chemical reaction occur. So just like a copilot helps a pilot fly a plane, a coenzyme helps an enzyme catalyze a chemical reaction. So that's really what most vitamins and minerals do.
We're going to tell you more about vitamins and minerals before we're done yet today. Now, what are enzyme inhibitors? I've now realized some people don't know what the word inhibit means.
Inhibit means to stop from working. So an enzyme inhibitor is something that stops an enzyme from working. And if you stop an enzyme from working, that could be pretty serious, assuming these chemical reactions are important.
How would an enzyme inhibitor work? Let's see. Look on the next page, A16.
And this time let's look at the bottom of the page, the bottom of A16. So on the bottom of page A16, this is our diagrammatic drawing of an enzyme. And this is labeled an inhibitor. Once this inhibitor attaches to the enzyme, now this enzyme is unable to attach to the normal substrate.
If this enzyme was sucrase, just like we saw above, If an inhibitor attaches to sucrase, then the sucrase is unable to attach to sucrose. So you've stopped that chemical reaction from occurring. Now again, some of these enzymatic chemical reactions... are absolutely essential to life.
So if you have a chemical that stops an enzyme from working, it probably, in some cases, might cause your death. So some enzyme inhibitors are also called poisons. You'd say, did you write that?
Yeah, I wrote it on page A15. So on the previous page, A15, that's why we wrote some enzyme inhibitors that when they stop an enzyme from working, basically are poisons that cause you to die. An example of that is one of the most lethal substances known.
It's called cyanide. Cyanide is almost surprising that it's so harmful. All it is is a carbon and nitrogen joined together. Carbon and nitrogen don't seem like very dangerous types of atoms. Many organic molecules in our body are made up of carbon and hydrogen and nitrogen and so on.
So it's surprising that it's so dangerous. How does cyanide work? Why is cyanide so dangerous? cyanide so lethal and it does cause death. Cyanide specifically attaches to an enzyme called cytochrome oxidase.
I don't care that you know the name of the enzyme, but it binds to this enzyme. You'd say, okay, so what? So then that enzyme can't work, right? That's right.
The enzyme can't work. So what is that enzyme for? This is an enzyme found in the mitochondria of all cells.
It is in the mitochondria commonly nicknamed the powerhouses of the cell where most cellular respiration occurs, where most ATP is produced. So cyanide basically interferes with the production of ATP. Remember ATP is that gasoline that powers cells. It interferes with the production of ATP in every single cell of the body. So literally every single cell starts to die because it's running out of gas in a sense.
Just like if you don't have gas in your car, it won't drive. If your cells can't make ATP, they stop working. They die.
Exposure to cyanide, if you inhale it, you'll be dead in four minutes. There is no antidote to cyanide. No antidote.
So that's an example of an enzyme inhibitor that pulls you out, that you die from. Some enzyme inhibitors are more subtle than that. We will be learning in the future about an enzyme called acetylcholinesterase.
Acetylcholinesterase is an enzyme in our nervous system. It's an enzyme in our nervous system. There are chemicals that interfere...
with this enzyme. They're called acetylcholinesterase inhibitors. They're called acetylcholinesterase inhibitors. They stop that enzyme from working.
With this enzyme, acetylcholinesterase doesn't work. it causes paralysis of all the muscles in our body, the skeletal muscles in our body. Not only can you not move your arms, not only can you not move your legs, but you're going to die. Now you'd say, well, why would I die?
You don't die just because you can't move your arms or legs. The most important skeletal muscle of the body is the diaphragm muscle. The diaphragm is a skeletal muscle.
You'll remember from it. anatomy you remember you learned there are three types of muscles or muscle tissues skeletal muscle this smooth muscle and cardiac muscle the most important of the skeletal muscles is the diaphragm muscle so not only can you not move your arm or leg muscles you can't breathe so it eventually causes death we'll talk more about not only acetylcholinesterase but acetylcholinesterase inhibitors when we get to the nervous system So, so far, incidentally, if there's any questions or anything you want me to slow down, just yell it out. Otherwise, I'll just keep rolling along. So far, you're thinking, okay, are we done with enzyme inhibitors? Like, who cares?
All right, fine, they kill you. That's all we need to know, right? Not exactly.
Not all enzyme inhibitors, you know, these chemicals like cyanide that stops the production of ATP, which is so essential, if you stop the production of ATP in the cells, you're going to die. But sometimes... We actually use enzyme inhibitors as medicines. You'd say, really? We're going to give you three examples.
On the next page, page A16. On A16, it says examples of enzyme inhibitors used in medicine. Incidentally, what I'm about to say would make a great short essay question.
Just a hint. All right? An example of an enzyme inhibitor are all antibiotics. All antibiotics are enzyme inhibitors. You'd say, what do you mean?
The way that penicillin works is penicillin and all the other of antibiotics inhibit bacterial enzymes. By inhibiting a bacterial enzyme, the bacteria dies. It's a poison to the bacteria. But since we don't have in our human cells that bacterial enzyme, the penicillin doesn't affect our cells.
So literally when you swallow penicillin, you're swallowing poison. But it's only poisonous to the bacteria. Now different antibiotics inhibit different bacterial enzymes. So that's why, and some of you have had microbiology, so you learn there are all kinds of different bacteria.
In microbiology you learn that there are gram positive aerobic bacteria. You learn that there are lycoxies. You learn that there are gram negative bacilli that are anaerobes. There are all kinds of different bacteria. So in fact.
We use different antibiotics to kill different types of bacteria. Depending upon which bacteria you want to kill, you use a different antibiotic. What's the difference between them? The enzyme they inhibit. All right, and different bacteria contain different enzymes.
So, and again, these antibiotics have very little effect on our cells because they don't affect any enzymes within our cells. They only affect the enzyme in bacteria. So now you know how antibiotics work. There are specific bacteria. Bacterial antibiotics that kill different bacteria.
There are antifungal antibiotics that kill fungal cells like nystat and monostat. All right. Another example we've already learned about last week. Aspirin and Advil, we wrote, inhibit the enzyme that converts phospholipids into prostaglandins. Did we talk about that last week?
Yes, we did. Let's show you the page. We'll just remind you. If you go back to page... page, yeah, page A9.
So back on page A9. On page A9, we learned last week that when cells are injured, an enzyme converts phospholipids in the cell membrane into prostaglandins. And prostaglandins cause... We learned that aspirin and Advil block the conversion of the phospholipids into prostaglandins. How do they do that?
They inhibit the enzyme that converts the phospholipids. lipids into prostaglandins. So in fact aspirin and Advil and all of the non-steroidal anti-inflammatory drugs are enzyme inhibitors. That's how they work.
Alright you'd say alright fine so I know how antibiotics work, I know how non-steroidal anti-inflammatory drugs work. Okay is that it? Back on page A16 a third example Lipitor and other statins inhibit the enzyme that can converts fatty acids into cholesterol. Did we talk about that last week?
We did. Let's go back to the page that we talked about it. It was page A11. On page A11 we wrote Lipitor, the most prescribed drug in the United States is an enzyme that is used to treat cancer. It inhibits an enzyme in your liver cells that converts saturated fats into cholesterol, thereby reducing the total amount of cholesterol formed in your body.
So in fact, the... The point that I'm really trying to make for all you future nurses and physician's assistants and pharmacists is that in fact many, many drugs are in fact enzyme inhibitors. That's how they work.
Alright, that takes us to page A17. On A17 we've been talking about enzymes and coenzymes and enzyme inhibitors. Another very important role of proteins, and we're not trying to be comprehensive right now, just make sure that you're not just talking about the whole thing. some of the most important Functions of proteins is there are protein hormones.
What's a hormone? Do we tell you what a hormone was? Huh? It's secreted in the blood.
Yes, it's a chemical that's secreted and circulates in your bloodstream that affects your body. Alright? Hormones circulate in our bloodstream. Now, we're talking about protein hormones. You might say, but Professor Fink, last week we talked about hormones already.
Last week we talked about steroid hormones. Today I'm talking about protein hormones. There are two major categories of hormones. Those that are steroids that are made from cholesterol and those that are protein hormones that are assembled or built from amino acids. You'd say, well, like, is that important that we know that it's a steroid made from cholesterol versus a protein made from amino acids?
It is. There are many, many differences between steroid hormones such as estrogen, such as glucocorticoid steroids, mineralocorticoid steroids, such as calcium. versus protein hormones like insulin or growth hormone or oxytocin. We're going to be learning a lot of differences between steroid hormones and protein hormones.
Here's one difference I'll mention right now. We wrote steroid hormones are not broken apart by the digestive system. Proteins are. Look, we have said that if you eat foods high in cholesterol, if you eat foods high in cholesterol, What's a food that's really high in cholesterol? Egg yolks.
You say, but you told us eggs are good. I said eggs are really good in terms of the good balance of essential amino acids. But they're not so good in terms of having high cholesterol levels.
Things are complicated. But when you eat cholesterol from eggs, from meat, we said anything from an animal has cholesterol, cholesterol is not broken apart. All that cholesterol that's in your food is is absorbed into your body.
Not only is cholesterol not digested but absorbed whole into your body, so are steroid hormones. Remember how steroid hormones look pretty much just like a cholesterol molecule? Remember we saw the pictures of them on page, I think it was A12? So when you swallow estrogen, you'd say, well, like, who swallows estrogen?
That's what's in a birth control pill. So when a woman takes a birth control pill containing estrogen and progesterone, these look like cholesterol, and you swallow it. it and they're absorbed whole right into the bloodstream, right into the body. So they're not digested or broken apart. On the other hand, anytime you swallow a protein, what happens to any protein that you swallow?
It's digested into amino acids. So if you swallow insulin, insulin is broken apart into amino acids. So steroid hormones can be taken orally by protein.
hormones cannot be taken orally they must be injected do you really think that a diabetic a kid a kid's a diabetic imagine and they have to inject themselves twice a day with insulin do you really think that the parent of that kid would say you know I know he could take a pill but I'd rather have him inject himself twice a day no parent would tell their kid to do that they don't have a choice if they take it if they swallow the insulin it won't work It's broken apart into amino acids. So it must be injected. All protein hormones must be injected in order to work.
You have to bypass the digestive system. All right, so that's one difference between protein hormones and steroid hormones. There are many other important differences we'll get to. Now, we're going to mention a few protein hormones, just like we mentioned a few steroid hormones.
There are many, many more. Now, insulin is produced by the beta cells of the pancreatic islet. In anatomy, what did you learn is so unique about the pancreas as an organ?
Yes, it's the only organ in the body that is both an endocrine gland and an exocrine gland. Now if you don't know the difference, look it up. You should have learned that in anatomy.
So it is both an endocrine gland and an exocrine gland. The pancreatic islets are the endocrine part of the pancreas and there are alpha cells and beta cells. The beta cells secrete insulin. Insulin is a hormone, it circulates in our bloodstream and it lowers our blood sugar level.
How does insulin lower our blood sugar level? It causes cells to transport sugars into the cell. As the insulin causes the cells to transport the sugar from the bloodstream into the cell, what's going to happen to the amount of sugar in your blood? It goes down. So insulin lowers the amount of sugar in your blood.
Now, which cells of our body are most important in storing sugars? and how our sugars are stored. Our liver cells and our muscle cells are especially important in absorbing sugars and storing them as a polysaccharide called glycogen. The normal glucose level in our blood is about 100 milligrams of glucose per deciliter of blood.
That number doesn't necessarily mean a lot to us now, but it will over time. Our first lab test is going to be dosage. calculations and explaining all these units that we use to quantify normal sugar levels, normal cholesterol levels, normal urea levels, normal protein levels in our body.
Because we have to quantify it. Now, if somebody doesn't produce enough insulin, we call that diabetes. Since insulin causes the sugar to go into the cells of our body, lowering the amount of sugar, if we don't produce enough...
insulin then the sugar just accumulates in our bloodstream and those levels of sugar in our bloodstream just get higher and higher and higher. Without the insulin you just have higher and higher and higher levels of sugar in our blood that's called hyperglycemia. Hyper means high. EMEA means, anybody know what EMEA means? In the blood.
EMEA means in the blood. So what is there high amounts of in the blood? Glyce, like the word glucose. High glucose in the blood.
That's the definition of diabetes. Diabetes is a high blood sugar level higher than the normal level. We actually talked about that on page A1.
If you don't believe me, look at A1. And we'll just do one more here before the break. Growth hormone. Now growth hormone is a protein hormone secreted by our pituitary gland. If you covered in anatomy, the two parts are...
lobes of the pituitary. Now I recognize some anatomy teachers talk about both lobes, others don't. If you had me, I talked about them. So it's released from the adenohypophysis of the pituitary gland, not the neurohypophysis. offices, but we'll review that later.
Alright? But from the pituitary gland. This is a protein hormone.
So if an individual needs growth hormone, can they just swallow a pill? No. It'll have to be injected.
All protein hormones must be injected. Well, they might as well just do oxytocin. Alright, oxytocin.
Oxytocin is another protein hormone. It's available under a brand name Pitocin. You may have heard of Pitocin. It's also secreted from the pituitary gland, but the neurohypophysis rather than the adenohypophysis. Oxytocin causes labor contractions of the uterus.
It causes a woman to go into labor. It causes her uterus to contract. So when they want to induce labor, they simply give an injection of Pitocin. It has to be injected.
Okay? Can't swallow a pill. It's a protein hormone, and within five minutes, she's in labor.
Okay? And that's it. This is not a comprehensive list of what all the proteins in our body do by any means, but antibodies are proteins.
Those of you who have had a microbiology class, learn the structure of an antibody. or an immunoglobulin. In fact, anything that ends in globin or globulin is a protein. Why does anything that ends in globin or globulin a protein?
Because they have this globular shape. All right? What's an example of a word that has the word globin?
Hemoglobin. What's an example, or myoglobin? What's an example of something that has the similar kind of ending globulin? Immunoglobulin.
These are proteins. So, in fact, the. or immunoglobulin or gamma globulin proteins, all those terms mean the same thing, is that they actually have a shape of the letter Y. And so those of you who have had a microbiology class learned all about the light chain and the heavy chain and the Y-shaped chain, the whole Y shape of an antibody protein. Antibodies are produced by the B-B-B lymphocytes.
There are different types of lymphocytes. I always try to remember that the B-B-B lymphocytes are the ones that are B lymphocytes are the ones that produce the antibodies because the T lymphocytes don't produce antibodies. They are involved in the cellular immune response and these antibodies inactivate foreign agents be they bacteria or viral particles or fungal cells or any foreign agent that enters our body.