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And we also have thirianine proteases. So let's very quickly discuss these four of the five protease molecules. So let's begin with serine proteases. And by the way, the major difference between these different proteases is the presence of a specific type of residue inside the active side of that enzyme. So in the case of seren proteasis from the name you might guess that inside that active side it's a serene molecule, a serine amino acid that plays the nucleochilic role of nucleophilically attacking or breaking that peptide bond. And so it's the serine that ultimately catalyzes that reaction. | Introduction to Proteases.txt |
And by the way, the major difference between these different proteases is the presence of a specific type of residue inside the active side of that enzyme. So in the case of seren proteasis from the name you might guess that inside that active side it's a serene molecule, a serine amino acid that plays the nucleochilic role of nucleophilically attacking or breaking that peptide bond. And so it's the serine that ultimately catalyzes that reaction. Now in addition to that serene, as we'll see in the next lecture, there are other additional residues present in the active side that also assist in the catalysis process as we'll discuss in the next lecture. Now, what are some examples of senior proteases and what are some of their roles? So let's begin with some digestive enzymes. | Introduction to Proteases.txt |
Now in addition to that serene, as we'll see in the next lecture, there are other additional residues present in the active side that also assist in the catalysis process as we'll discuss in the next lecture. Now, what are some examples of senior proteases and what are some of their roles? So let's begin with some digestive enzymes. So we have trypsin, we have chimetrypsin, we also have elastase. And these three are digestive enzymes found inside our small intestine which basically play the role of breaking down the proteins that we ingest. We also have cum proteases involved in the blood coagulation process and we'll discuss these in much more detail when we'll discuss the blood cascade. | Introduction to Proteases.txt |
So we have trypsin, we have chimetrypsin, we also have elastase. And these three are digestive enzymes found inside our small intestine which basically play the role of breaking down the proteins that we ingest. We also have cum proteases involved in the blood coagulation process and we'll discuss these in much more detail when we'll discuss the blood cascade. And so these are thrombin and plasmid. Now inside our immune system we have the complement system and one important serum protease, part of the complement system is known as the complement C one. And finally, serum proteases also play a role in reproduction. | Introduction to Proteases.txt |
And so these are thrombin and plasmid. Now inside our immune system we have the complement system and one important serum protease, part of the complement system is known as the complement C one. And finally, serum proteases also play a role in reproduction. So when we discuss sperm cells, we said that on the tip of sperm cells are these structures we call acrosomes. And inside the acrosomes are digestive enzymes and these digestive enzymes are known as acrosoma proteases. And these are examples of serene proteases. | Introduction to Proteases.txt |
So when we discuss sperm cells, we said that on the tip of sperm cells are these structures we call acrosomes. And inside the acrosomes are digestive enzymes and these digestive enzymes are known as acrosoma proteases. And these are examples of serene proteases. So serene proteases are involved in biological processes such as digestion. So trypsin chymatripsin, elastase, blood coagulation, thrombin and plasma. We have immunity, so the complement C one. | Introduction to Proteases.txt |
So serene proteases are involved in biological processes such as digestion. So trypsin chymatripsin, elastase, blood coagulation, thrombin and plasma. We have immunity, so the complement C one. And we also have reproduction, namely acrosoma protease which are the enzymes which are needed to basically digest a hole inside the membrane covering of that excel so the sperm cell can move inside that X cell to form that zygote. Now, we also have not only serum proteases, we have cysteine proteases aspertal or aspartate proteases and metalloprotiases. So as you might infer from the title, cysteine proteases basically contain a cysteine residue that plays that nucleosilic role of attacking that peptide bond and catalyzing this hydrolysis reaction. | Introduction to Proteases.txt |
And we also have reproduction, namely acrosoma protease which are the enzymes which are needed to basically digest a hole inside the membrane covering of that excel so the sperm cell can move inside that X cell to form that zygote. Now, we also have not only serum proteases, we have cysteine proteases aspertal or aspartate proteases and metalloprotiases. So as you might infer from the title, cysteine proteases basically contain a cysteine residue that plays that nucleosilic role of attacking that peptide bond and catalyzing this hydrolysis reaction. Now, cysteine proteases such as cat space and cathepsen are involved in programmed cell death, also known as epitosis. And this is basically an immune response that our body has. And this process is also involved in a normal embryological development of that human embryo. | Introduction to Proteases.txt |
Now, cysteine proteases such as cat space and cathepsen are involved in programmed cell death, also known as epitosis. And this is basically an immune response that our body has. And this process is also involved in a normal embryological development of that human embryo. Now, other evidence also suggests that we have 16 proteases that are involved in bone remodeling as well as MHC class two processing. And remember, MHC class two is a protein complex found on certain cells, immune cells of our body where MHC stands for the major historic compatibility class two complex. Now, these cysteine proteases are also found in many other organisms and they are found predominantly in fruits. | Introduction to Proteases.txt |
Now, other evidence also suggests that we have 16 proteases that are involved in bone remodeling as well as MHC class two processing. And remember, MHC class two is a protein complex found on certain cells, immune cells of our body where MHC stands for the major historic compatibility class two complex. Now, these cysteine proteases are also found in many other organisms and they are found predominantly in fruits. And so papaya type of fruit contains a special cysteine protease known as papain. Now let's move on to aspartyl or aspartate proteases as well as metallic proteases. So once again from the title, from that name you can infer that instead of having Serene or cysteine inside these active sites of these enzymes, we have aspartic acid. | Introduction to Proteases.txt |
And so papaya type of fruit contains a special cysteine protease known as papain. Now let's move on to aspartyl or aspartate proteases as well as metallic proteases. So once again from the title, from that name you can infer that instead of having Serene or cysteine inside these active sites of these enzymes, we have aspartic acid. In fact, these enzymes contain two so a pair of aspartic acids. And as we'll discuss in a future lecture, one of those residues takes away an H atom and the other residue basically is used to increase the nucleophilic character of that particular substrate molecule. And Renan or Renin is basically an example of an aspartal protease that is involved in increasing or decreasing so regulating the blood pressure inside our body. | Introduction to Proteases.txt |
In fact, these enzymes contain two so a pair of aspartic acids. And as we'll discuss in a future lecture, one of those residues takes away an H atom and the other residue basically is used to increase the nucleophilic character of that particular substrate molecule. And Renan or Renin is basically an example of an aspartal protease that is involved in increasing or decreasing so regulating the blood pressure inside our body. And we also have another example, namely Pepsin. And Pepsin is once again an example of a digestive enzyme. It's used to break down the proteins that we ingest into our body. | Introduction to Proteases.txt |
And we also have another example, namely Pepsin. And Pepsin is once again an example of a digestive enzyme. It's used to break down the proteins that we ingest into our body. And finally we have metalloprotease. And these are simply enzymes proteases that actually utilize a metal atom, a metal ion to basically catalyze that hydrolysis reaction. And two examples of such metalloproteases are carboxy peptidis a which an example of a digestive enzyme. | Introduction to Proteases.txt |
Now I'd like to focus on a signal transduction pathway that involves insulin. Now, before we take a look at the details of the pathway, let's discuss what insulin is, what it does and when our body actually uses it. So let's suppose we just had a meal and the meal is rich in carbohydrates. And what that means is our body will begin to break down the carbohydrates, the polysaccharides, into their individual units, glucose molecules. And so following a meal that is rich in carbohydrates, we see that inside our blood, the glucose levels will begin to increase. And the rise in concentration of glucose in the blood can actually be very dangerous, very toxic to our body. | Insulin Signal Transduction Pathway .txt |
And what that means is our body will begin to break down the carbohydrates, the polysaccharides, into their individual units, glucose molecules. And so following a meal that is rich in carbohydrates, we see that inside our blood, the glucose levels will begin to increase. And the rise in concentration of glucose in the blood can actually be very dangerous, very toxic to our body. And so what the body does is it responds by stimulating the beta cells of the eyelids of Langerhine that are part of the pancreas to release insulin molecules into the blood. And insulin is a small peptide hormone. Now, what insulin does is it initiates this signal transduction pathway. | Insulin Signal Transduction Pathway .txt |
And so what the body does is it responds by stimulating the beta cells of the eyelids of Langerhine that are part of the pancreas to release insulin molecules into the blood. And insulin is a small peptide hormone. Now, what insulin does is it initiates this signal transduction pathway. And the signal transduction pathway is actually very complicated, very complex and very extensive. And so what I'd like to focus on in this lecture is actually a small section of this insulin signal transduction pathway that stimulates the absorption of the glucose by the cells and a subsequent transformation of the glucose into the glycogen form. So this is what I'd like to focus on in this lecture. | Insulin Signal Transduction Pathway .txt |
And the signal transduction pathway is actually very complicated, very complex and very extensive. And so what I'd like to focus on in this lecture is actually a small section of this insulin signal transduction pathway that stimulates the absorption of the glucose by the cells and a subsequent transformation of the glucose into the glycogen form. So this is what I'd like to focus on in this lecture. So let's see exactly how that takes place. Now, let's begin by focusing on the structure of the receptor that actually binds insulin. So insulin binds onto a receptor we call the insulin receptor. | Insulin Signal Transduction Pathway .txt |
So let's see exactly how that takes place. Now, let's begin by focusing on the structure of the receptor that actually binds insulin. So insulin binds onto a receptor we call the insulin receptor. And the insulin receptor actually is a diamond that consists of two identical chains, one chain and a second identical chain. And each one of these chains themselves consists of two individual units. We have the alpha unit shown here in purple, and this beta unit shown here in pink. | Insulin Signal Transduction Pathway .txt |
And the insulin receptor actually is a diamond that consists of two identical chains, one chain and a second identical chain. And each one of these chains themselves consists of two individual units. We have the alpha unit shown here in purple, and this beta unit shown here in pink. Now, the alpha unit is attached onto the beta unit by a disulfide bridge shown here. So we have one bridge shown here and another bridge shown on that adjacent identical chain. Now, what exactly is the function of the alpha and the beta units? | Insulin Signal Transduction Pathway .txt |
Now, the alpha unit is attached onto the beta unit by a disulfide bridge shown here. So we have one bridge shown here and another bridge shown on that adjacent identical chain. Now, what exactly is the function of the alpha and the beta units? Well, the two alpha units, which are, by the way, found on the outside of the cell, the extracellular environment basically create the pocket, the region of space that binds the insulin. And so that exists on the outside of the cell. Now, these beta submunes not only spam the entire membrane shown here, but they also have components found on the inside the cytoplasmic side of the cell. | Insulin Signal Transduction Pathway .txt |
Well, the two alpha units, which are, by the way, found on the outside of the cell, the extracellular environment basically create the pocket, the region of space that binds the insulin. And so that exists on the outside of the cell. Now, these beta submunes not only spam the entire membrane shown here, but they also have components found on the inside the cytoplasmic side of the cell. And these two regions of the beta soviets basically contain a very important section that gives this receptor its activity. And this section contains the tyrosine protein kinase domains. Now, a tyrosine protein kinase is basically an enzyme, a protein that phosphorylates tyrosine amino acids on target proteins and enzymes. | Insulin Signal Transduction Pathway .txt |
And these two regions of the beta soviets basically contain a very important section that gives this receptor its activity. And this section contains the tyrosine protein kinase domains. Now, a tyrosine protein kinase is basically an enzyme, a protein that phosphorylates tyrosine amino acids on target proteins and enzymes. And we'll see what those are used for in just a moment. So this is what the insulin receptor actually looks like. Now, notice there's an important difference between this insulin receptor and the receptors that we spoke of previously. | Insulin Signal Transduction Pathway .txt |
And we'll see what those are used for in just a moment. So this is what the insulin receptor actually looks like. Now, notice there's an important difference between this insulin receptor and the receptors that we spoke of previously. So, for instance, in our discussion on the epinephrine signaling pathway we said that that pathway actually uses G proteins and those receptors are known as G coupled protein receptors. But in this particular case, for the case of insulin we don't actually use any G proteins. Instead, we actually have protein kinases found within the structure of this receptor. | Insulin Signal Transduction Pathway .txt |
So, for instance, in our discussion on the epinephrine signaling pathway we said that that pathway actually uses G proteins and those receptors are known as G coupled protein receptors. But in this particular case, for the case of insulin we don't actually use any G proteins. Instead, we actually have protein kinases found within the structure of this receptor. Now, what happens when the insulin actually binds? So insulin is the primary messenger of this particular pathway and the insulin shown in orange binds into this cavity that is created by these two alpha units. And once the insulin actually moves in these two structures the alpha units actually close in. | Insulin Signal Transduction Pathway .txt |
Now, what happens when the insulin actually binds? So insulin is the primary messenger of this particular pathway and the insulin shown in orange binds into this cavity that is created by these two alpha units. And once the insulin actually moves in these two structures the alpha units actually close in. And as they close in, they seal off this region so that the insulin cannot actually detach. On top of that, they also cause these two beta subunits to basically move closer together. Now, as these two beta subunits move closer together the activation region of one of the beta subunits actually moves into the active side of the other beta Subun. | Insulin Signal Transduction Pathway .txt |
And as they close in, they seal off this region so that the insulin cannot actually detach. On top of that, they also cause these two beta subunits to basically move closer together. Now, as these two beta subunits move closer together the activation region of one of the beta subunits actually moves into the active side of the other beta Subun. And this causes a cross phosphorylation process in which both of these beta units are actually phosphorylated in the presence of ATP. And what that does is it activates this insulin receptor. And because of the fact that this receptor itself contains a tyrosine protein kinase we also called the insulin receptor, the insulin receptor protein kinase. | Insulin Signal Transduction Pathway .txt |
And this causes a cross phosphorylation process in which both of these beta units are actually phosphorylated in the presence of ATP. And what that does is it activates this insulin receptor. And because of the fact that this receptor itself contains a tyrosine protein kinase we also called the insulin receptor, the insulin receptor protein kinase. So once again, when the insulin primary messenger, a peptide hormone, moves into its cavity that is created by the two alpha subunits the closure of the two alpha chains causes the two beta chains to move closer together and this leads to crossfosphorylation as shown here and here. That basically changes the confirmation of those beta subunits and that activates those beta subunits. So we see the binding of the insulin on one side of that receptor activates it on the other side and so that signal can basically be transduced passed down from the outside to the inside of that cell. | Insulin Signal Transduction Pathway .txt |
So once again, when the insulin primary messenger, a peptide hormone, moves into its cavity that is created by the two alpha subunits the closure of the two alpha chains causes the two beta chains to move closer together and this leads to crossfosphorylation as shown here and here. That basically changes the confirmation of those beta subunits and that activates those beta subunits. So we see the binding of the insulin on one side of that receptor activates it on the other side and so that signal can basically be transduced passed down from the outside to the inside of that cell. Now, what actually happens when these two regions are phosphorylated? So this beta submune and the other beta submune well, remember, what the tyrosine protein kinase does is it phosphorylates. It attaches a phosphoryl group onto tyrosine residues and some of these tyrosine residues that are phosphorylated actually begin to act as attachment points for other proteins namely an important protein known as IRS which stands for insulin receptor substrate. | Insulin Signal Transduction Pathway .txt |
Now, what actually happens when these two regions are phosphorylated? So this beta submune and the other beta submune well, remember, what the tyrosine protein kinase does is it phosphorylates. It attaches a phosphoryl group onto tyrosine residues and some of these tyrosine residues that are phosphorylated actually begin to act as attachment points for other proteins namely an important protein known as IRS which stands for insulin receptor substrate. So one of the phosphorylated tyrosine residues on the insulin receptor more specifically this one over here basically attracts a protein called the insulin receptor substrate or simply IRS. And once the IRS and in this particular case, we call it IRS One because we actually have another one called IRS Two which exists in a different pathway that we're not going to look in this lecture. But IRS One basically attaches onto this phosphorylated residue and once it is attached because it moves in close proximity to the active side of that activated receptor kinase. | Insulin Signal Transduction Pathway .txt |
So one of the phosphorylated tyrosine residues on the insulin receptor more specifically this one over here basically attracts a protein called the insulin receptor substrate or simply IRS. And once the IRS and in this particular case, we call it IRS One because we actually have another one called IRS Two which exists in a different pathway that we're not going to look in this lecture. But IRS One basically attaches onto this phosphorylated residue and once it is attached because it moves in close proximity to the active side of that activated receptor kinase. This green structure, the IRS itself is phosphorylated at four tyrosine residues. So upon binding, the IRS itself is phosphorylated by the insulin receptor kinase. Now, what is the point of asphorylating this region? | Insulin Signal Transduction Pathway .txt |
This green structure, the IRS itself is phosphorylated at four tyrosine residues. So upon binding, the IRS itself is phosphorylated by the insulin receptor kinase. Now, what is the point of asphorylating this region? And in general, what exactly is the function of the IRS one structure? Well, the IRS protein is not actually a protein that activates something in the pathway. Instead, what it does is it functions as an adaptive protein. | Insulin Signal Transduction Pathway .txt |
And in general, what exactly is the function of the IRS one structure? Well, the IRS protein is not actually a protein that activates something in the pathway. Instead, what it does is it functions as an adaptive protein. So IRS molecules are called adaptive proteins. Why? Well, because instead of activating anything, they actually act as attachment points for other enzymes, other proteins. | Insulin Signal Transduction Pathway .txt |
So IRS molecules are called adaptive proteins. Why? Well, because instead of activating anything, they actually act as attachment points for other enzymes, other proteins. So instead the phosphorylated IRS. So instead of activating anything, they phosphorylates the phosphorylated. IRS basically acts as an attachment point for a lipid kinase. | Insulin Signal Transduction Pathway .txt |
So instead the phosphorylated IRS. So instead of activating anything, they phosphorylates the phosphorylated. IRS basically acts as an attachment point for a lipid kinase. And remember, lipid kinases are protein kinase that take a phosphoryl group from ATP and they move it onto some type of fat molecule, some type of lipid molecule. And to be more specific, the lipid kinase that this actually attaches to is known as phosphonosatide three kinase. So we have the phosphorylation of these four residues on this iris molecule causes this molecule here, phosphorositi Three kinase to actually attach. | Insulin Signal Transduction Pathway .txt |
And remember, lipid kinases are protein kinase that take a phosphoryl group from ATP and they move it onto some type of fat molecule, some type of lipid molecule. And to be more specific, the lipid kinase that this actually attaches to is known as phosphonosatide three kinase. So we have the phosphorylation of these four residues on this iris molecule causes this molecule here, phosphorositi Three kinase to actually attach. So the phosphorusati three kinase contains a regulatory region, shown here, that attaches onto the phosphorylated residue of the IRS molecule. And once this attachment takes place, that causes the active side of this lipid kinase to move in in close proximity with respect to the membrane. So this is the active side of this phosphor nosetide kinase. | Insulin Signal Transduction Pathway .txt |
So the phosphorusati three kinase contains a regulatory region, shown here, that attaches onto the phosphorylated residue of the IRS molecule. And once this attachment takes place, that causes the active side of this lipid kinase to move in in close proximity with respect to the membrane. So this is the active side of this phosphor nosetide kinase. And once that active side moves there, it causes the phosphorylation of a specific type of fat molecule that exists within the membrane known as Pip two. Now, when did we see Pip Two previously? Well, we actually spoke about Pip Two in our discussion on the phosphornosatide cascade. | Insulin Signal Transduction Pathway .txt |
And once that active side moves there, it causes the phosphorylation of a specific type of fat molecule that exists within the membrane known as Pip two. Now, when did we see Pip Two previously? Well, we actually spoke about Pip Two in our discussion on the phosphornosatide cascade. And we said that Pip two, Pip Two stands for phosphatididylin nosetal 45 diphosphate. So this molecule contains a polar region that points towards the cytoplasmic side and a non polar region that consists of two tails that lies within the membrane. Now, what this lipid kinase does is it basically attaches a phosphoryl group. | Insulin Signal Transduction Pathway .txt |
And we said that Pip two, Pip Two stands for phosphatididylin nosetal 45 diphosphate. So this molecule contains a polar region that points towards the cytoplasmic side and a non polar region that consists of two tails that lies within the membrane. Now, what this lipid kinase does is it basically attaches a phosphoryl group. It takes a phosphoryl group from an ATP molecule and it places that phosphoryl group onto the Pip two and that creates Pip Three. So Pip Two stands for phosphatidolinotitol four, five, diphosphate, but Pip Three stands for phosphateidolinosatoll three, four, five triphosphate. And so we see that this phosphor noseattype three kinase phosphorylates the third carbon on this Pip Two to form the Pip three. | Insulin Signal Transduction Pathway .txt |
It takes a phosphoryl group from an ATP molecule and it places that phosphoryl group onto the Pip two and that creates Pip Three. So Pip Two stands for phosphatidolinotitol four, five, diphosphate, but Pip Three stands for phosphateidolinosatoll three, four, five triphosphate. And so we see that this phosphor noseattype three kinase phosphorylates the third carbon on this Pip Two to form the Pip three. And once we form the Pip three, the Pip Three basically moves along the membrane and eventually ends up on a protein known as Pip Three. So pip three dependent protein kinase. And once it binds onto this protein kinase, this protein kinase, shown in green, is able to activate an important effect of molecule important protein kinase known as protein kinase B, also known as AKT. | Insulin Signal Transduction Pathway .txt |
And once we form the Pip three, the Pip Three basically moves along the membrane and eventually ends up on a protein known as Pip Three. So pip three dependent protein kinase. And once it binds onto this protein kinase, this protein kinase, shown in green, is able to activate an important effect of molecule important protein kinase known as protein kinase B, also known as AKT. So we see that phosphor, nototide three kinase, phosphorylates the Pip Two into Pip three that then travels along the membrane to activate a protein kinase we call Pip Three dependent protein kinase or simply PDK One. So this is PDK One and once PDK is activated by the binding of the Pip Three to this kinase, it then goes on and activates this structure here, which is the inactive form of protein kinaseb also known as AKT. So AKT One is activated and once this is activated, it can basically diffuse across the cell membrane. | Insulin Signal Transduction Pathway .txt |
So we see that phosphor, nototide three kinase, phosphorylates the Pip Two into Pip three that then travels along the membrane to activate a protein kinase we call Pip Three dependent protein kinase or simply PDK One. So this is PDK One and once PDK is activated by the binding of the Pip Three to this kinase, it then goes on and activates this structure here, which is the inactive form of protein kinaseb also known as AKT. So AKT One is activated and once this is activated, it can basically diffuse across the cell membrane. So this protein kinase B, AKT, is not actually bound to the cell membrane and it can move anywhere within the cytoplasm of that particular cell. And what this AKT does is what the protein kinase B does is two things. It actually activates enzymes which are responsible for transforming glucose into Glycogen and it also stimulates these protein transporters to move into the membrane and cause the reabsorption of glucose into the cell. | Insulin Signal Transduction Pathway .txt |
So this protein kinase B, AKT, is not actually bound to the cell membrane and it can move anywhere within the cytoplasm of that particular cell. And what this AKT does is what the protein kinase B does is two things. It actually activates enzymes which are responsible for transforming glucose into Glycogen and it also stimulates these protein transporters to move into the membrane and cause the reabsorption of glucose into the cell. So we see that the PDK One then activates the protein kinase B we also call AKT. And this kinase is not membrane down and it can move anywhere around that cell. And it does two things. | Insulin Signal Transduction Pathway .txt |
So we see that the PDK One then activates the protein kinase B we also call AKT. And this kinase is not membrane down and it can move anywhere around that cell. And it does two things. It stimulates the movement of glucose membrane transporters to that cell membrane, which increases the uptake of glucose from the blood and into the cytoplasm of that cell. And once the glucose is inside the cell, that this same AKT alsophosphorylates to activate specific enzymes which are responsible for actually transforming those glucose molecules into Glycogen molecules. So the Glycogen can actually be stored in cells such as skeletal muscle cells and fat cells and so forth. | Insulin Signal Transduction Pathway .txt |
In our previous discussion we focus on the following graph and we said that the graph describes how the rate of the enzyme in an enzyme catalyze reaction changes when we change when we increase the substrate concentration. So as we increase the substrate concentration, as we make the Xvalue greater we see that the yvalue, the reaction velocity v naught, the rate at which the enzyme catalyzed the reaction basically increases and it follows the following blue curve. So initially at the beginning of that reaction, we have a relatively straight line, a straight slope, and then the slope begins to decrease and it levels off and eventually it begins to approach asymptotically the maximum velocity, the maximum rate of that enzymes activity, this red horizontal line. And notice the blue curve is never going to pass that v max value. Now, we also were able to actually derive the equation, the mathematical expression that describes the blue curve and this is known as the Michaelis Methan equation and this is the Michaelis Methane equation. So this equation describes this blue curve here. | Michaelis menten Equation .txt |
And notice the blue curve is never going to pass that v max value. Now, we also were able to actually derive the equation, the mathematical expression that describes the blue curve and this is known as the Michaelis Methan equation and this is the Michaelis Methane equation. So this equation describes this blue curve here. So v knot is the y coordinate. That's the velocity, the rate at which the enzyme catalyzes that reaction. And this is equal to the product of a constant V max. | Michaelis menten Equation .txt |
So v knot is the y coordinate. That's the velocity, the rate at which the enzyme catalyzes that reaction. And this is equal to the product of a constant V max. This Y value here multiplied by this ratio, the substrate concentration, the X value divided by Km, the Mikaela's constant. Plus, once again, the X value, the substrate concentration. Now, what we want to explore in this lecture is the meaning behind this equation. | Michaelis menten Equation .txt |
This Y value here multiplied by this ratio, the substrate concentration, the X value divided by Km, the Mikaela's constant. Plus, once again, the X value, the substrate concentration. Now, what we want to explore in this lecture is the meaning behind this equation. What physiological meaning does this equation actually have and does this equation correctly describe this blue curve? So this is what we basically want to answer in this question. Now what we want to explore first is the meaning behind the Km terms. | Michaelis menten Equation .txt |
What physiological meaning does this equation actually have and does this equation correctly describe this blue curve? So this is what we basically want to answer in this question. Now what we want to explore first is the meaning behind the Km terms. So Km is known as the Michaela's constant. The question is what is the physiological meaning of this Km value? Well, to answer this question we're going to begin by making a simplification. | Michaelis menten Equation .txt |
So Km is known as the Michaela's constant. The question is what is the physiological meaning of this Km value? Well, to answer this question we're going to begin by making a simplification. And the reason we want to make the simplification is to basically figure out the meaning behind Km. Now, because Km appears in the denominator we can see that the units of Km are the same as that for the concentration of the substrate. And so what we're going to assume initially is we're going to set the Km value equal to the substrate concentration and we'll see why we do that in just a moment. | Michaelis menten Equation .txt |
And the reason we want to make the simplification is to basically figure out the meaning behind Km. Now, because Km appears in the denominator we can see that the units of Km are the same as that for the concentration of the substrate. And so what we're going to assume initially is we're going to set the Km value equal to the substrate concentration and we'll see why we do that in just a moment. So if we set Km equal to the substrate concentration then this denominator can be simplified from Km plus this to simply the concentration of S plus the concentration of S, where Km has been replaced with the concentration of S. So V naught is equal to v max multiplied by this ratio. Now, the denominator can be combined to basically combine these two quantities. So it's as if we have x plus x and that gives us two x. | Michaelis menten Equation .txt |
So if we set Km equal to the substrate concentration then this denominator can be simplified from Km plus this to simply the concentration of S plus the concentration of S, where Km has been replaced with the concentration of S. So V naught is equal to v max multiplied by this ratio. Now, the denominator can be combined to basically combine these two quantities. So it's as if we have x plus x and that gives us two x. So that means we have v max multiplied by the concentration of S divided by two multiplied by the concentration of S. And notice these two quantities can now be canceled out and we simply have v Naught is equal to v max divided by two. And this is a very important physiological it carries very important physiological meaning. What this tells us is when the Michael is constant is equal to the substrate concentration, that particular x value, we see that the rate of that enzyme, the velocity of that enzyme is exactly half of the maximum velocity of that enzyme. | Michaelis menten Equation .txt |
So that means we have v max multiplied by the concentration of S divided by two multiplied by the concentration of S. And notice these two quantities can now be canceled out and we simply have v Naught is equal to v max divided by two. And this is a very important physiological it carries very important physiological meaning. What this tells us is when the Michael is constant is equal to the substrate concentration, that particular x value, we see that the rate of that enzyme, the velocity of that enzyme is exactly half of the maximum velocity of that enzyme. So if we look on the following y axis, this is the maximum velocity, this is the zero velocity. So the velocity in the middle is the v max divided by two. And if we draw that horizontal line and when that line touches that curve, we then draw a vertical line down that gives us the Y coordinate known as the Michael's constant Km. | Michaelis menten Equation .txt |
So if we look on the following y axis, this is the maximum velocity, this is the zero velocity. So the velocity in the middle is the v max divided by two. And if we draw that horizontal line and when that line touches that curve, we then draw a vertical line down that gives us the Y coordinate known as the Michael's constant Km. So basically the Mikala's constant Km describes the substrate concentration, the x value at which the rate, the velocity of that enzyme's activity is exactly half of its maximum velocity, v max. So if Km is equal to the substrate concentration, then V Naught is equal to v max divided by two. So that's the meaning behind Km. | Michaelis menten Equation .txt |
So basically the Mikala's constant Km describes the substrate concentration, the x value at which the rate, the velocity of that enzyme's activity is exactly half of its maximum velocity, v max. So if Km is equal to the substrate concentration, then V Naught is equal to v max divided by two. So that's the meaning behind Km. Km basically describes the situation when exactly half of all the active sites are filled with the substrate. And we'll talk much more about that in the next lecture. Now let's move on to two and three. | Michaelis menten Equation .txt |
Km basically describes the situation when exactly half of all the active sites are filled with the substrate. And we'll talk much more about that in the next lecture. Now let's move on to two and three. In two and three, we basically want to show that this Mikayla's methane equation actually correctly describes this blue curve here. So let's begin by going to the beginning of that chemical reaction. So at the beginning of the chemical reaction at a time of approximately zero, we know that the substrate concentration is very, very low. | Michaelis menten Equation .txt |
In two and three, we basically want to show that this Mikayla's methane equation actually correctly describes this blue curve here. So let's begin by going to the beginning of that chemical reaction. So at the beginning of the chemical reaction at a time of approximately zero, we know that the substrate concentration is very, very low. So the substrate concentration is somewhere around this value here at the beginning of that chemical reaction. Now let's compare the substrate concentration at the beginning to the Km value. Clearly the Km has a much higher value than the substrate concentration at the beginning. | Michaelis menten Equation .txt |
So the substrate concentration is somewhere around this value here at the beginning of that chemical reaction. Now let's compare the substrate concentration at the beginning to the Km value. Clearly the Km has a much higher value than the substrate concentration at the beginning. And so we're going to begin by making the following assumption. So when the time is approximately equal to zero at the beginning of that chemical reaction, the Km value is much greater than the concentration of that substrate. And so what that means is this sum, the Km value plus the substrate concentration is simply approximately equal to the Km value because this is much greater than this. | Michaelis menten Equation .txt |
And so we're going to begin by making the following assumption. So when the time is approximately equal to zero at the beginning of that chemical reaction, the Km value is much greater than the concentration of that substrate. And so what that means is this sum, the Km value plus the substrate concentration is simply approximately equal to the Km value because this is much greater than this. This is approximately equal to zero compared to this. And so Km is approximately Km plus the subsequent is approximately equal to Km. So this is approximately equal to zero. | Michaelis menten Equation .txt |
This is approximately equal to zero compared to this. And so Km is approximately Km plus the subsequent is approximately equal to Km. So this is approximately equal to zero. Now the point of making this simplification was to basically simplify this equation because what we actually want to do in step two is we actually want to describe the equation that describes how the curve behaves at the beginning of that particular reaction. So V Naught is equal to v max multiplied by this ratio. And because our denominator is Km plus the subsid concentration and as a result of this assumption we see that our denominator simply becomes Km. | Michaelis menten Equation .txt |
Now the point of making this simplification was to basically simplify this equation because what we actually want to do in step two is we actually want to describe the equation that describes how the curve behaves at the beginning of that particular reaction. So V Naught is equal to v max multiplied by this ratio. And because our denominator is Km plus the subsid concentration and as a result of this assumption we see that our denominator simply becomes Km. So this is approximately equal to v max multiplied by the substrate concentration divided by Km. Now instead of having the Km underneath this term, let's bring it underneath the V max term. And this is the equation that we have. | Michaelis menten Equation .txt |
So this is approximately equal to v max multiplied by the substrate concentration divided by Km. Now instead of having the Km underneath this term, let's bring it underneath the V max term. And this is the equation that we have. And so this equation is the equation that describes activity the rate of that enzyme at the beginning of that chemical reaction. And notice what this equation actually looks like. So based on the curve here, we see that at the beginning of the reaction, the curve. | Michaelis menten Equation .txt |
And so this equation is the equation that describes activity the rate of that enzyme at the beginning of that chemical reaction. And notice what this equation actually looks like. So based on the curve here, we see that at the beginning of the reaction, the curve. So from about this point in time to, let's say about this point in time, the curve looks like a straight line. And in fact, this equation also describes an equation that looks like a straight line. So remember, a straight line has the following general form. | Michaelis menten Equation .txt |
So from about this point in time to, let's say about this point in time, the curve looks like a straight line. And in fact, this equation also describes an equation that looks like a straight line. So remember, a straight line has the following general form. So y, the Y coordinate is equal to and the slope multiplied by x the x coordinate plus b the y intercept. Now B in this particular case is zero. So this is zero and it cancels out. | Michaelis menten Equation .txt |
So y, the Y coordinate is equal to and the slope multiplied by x the x coordinate plus b the y intercept. Now B in this particular case is zero. So this is zero and it cancels out. Now M is the slope that's v max divided by Km, x is a substrate concentration and Y is simply the velocity, the rate of that enzyme. So we see that this equation correctly describes the behavior of the enzyme at the beginning of that reaction. Not only that, but this equation also describes a reaction that has first order. | Michaelis menten Equation .txt |
Now M is the slope that's v max divided by Km, x is a substrate concentration and Y is simply the velocity, the rate of that enzyme. So we see that this equation correctly describes the behavior of the enzyme at the beginning of that reaction. Not only that, but this equation also describes a reaction that has first order. So remember in our discussion on the rate law we said that if the rate law looks like this, then our reaction is in fact a first order reaction where V is the rate of that particular reaction, k is the rate constant and this is a substitute concentration. And this coefficient, this exponent of one basically describes a first order reaction. And this looks like this or this looks like this where V is v naught, k is V max divided by Km and this quantity is equal to this. | Michaelis menten Equation .txt |
So remember in our discussion on the rate law we said that if the rate law looks like this, then our reaction is in fact a first order reaction where V is the rate of that particular reaction, k is the rate constant and this is a substitute concentration. And this coefficient, this exponent of one basically describes a first order reaction. And this looks like this or this looks like this where V is v naught, k is V max divided by Km and this quantity is equal to this. So what that basically means is at the beginning of that chemical reaction we see that the rate, the velocity of that enzymes activity is directly proportional to the substrate concentration. So that is what we mean by a first order reaction. So notice that this is a straight line and also a first order reaction. | Michaelis menten Equation .txt |
So what that basically means is at the beginning of that chemical reaction we see that the rate, the velocity of that enzymes activity is directly proportional to the substrate concentration. So that is what we mean by a first order reaction. So notice that this is a straight line and also a first order reaction. And this implies that the rate of the reaction is directly proportional to the substrate concentration at the beginning of that chemical reaction. So this equation correctly describes the behavior at the beginning of that chemical reaction. Now what about at the end of the chemical reaction? | Michaelis menten Equation .txt |
And this implies that the rate of the reaction is directly proportional to the substrate concentration at the beginning of that chemical reaction. So this equation correctly describes the behavior at the beginning of that chemical reaction. Now what about at the end of the chemical reaction? So in part two we basically discussed when the substrate concentration was very low. But what if the substrate concentration is very high? Can this equation correctly describe the behavior of that particular enzyme? | Michaelis menten Equation .txt |
So in part two we basically discussed when the substrate concentration was very low. But what if the substrate concentration is very high? Can this equation correctly describe the behavior of that particular enzyme? And this is what we do in part three. So we can also use the Michael's Methane equation to describe the enzyme activity towards the end of that reaction. So when the substrate concentration is very, very high. | Michaelis menten Equation .txt |
And this is what we do in part three. So we can also use the Michael's Methane equation to describe the enzyme activity towards the end of that reaction. So when the substrate concentration is very, very high. So now we're basically going to use the same argument as in this case, but we're going to reverse because at the end of the reaction so when we have a very, very high concentration of substrate that means the Km value is much smaller than the substrate concentration. So for example, if we're somewhere here along the X axis, this quantity, this concentration is much higher than Km. And so what that means is towards the end we see that the concentration of S is much, much higher than the value of Km. | Michaelis menten Equation .txt |
So now we're basically going to use the same argument as in this case, but we're going to reverse because at the end of the reaction so when we have a very, very high concentration of substrate that means the Km value is much smaller than the substrate concentration. So for example, if we're somewhere here along the X axis, this quantity, this concentration is much higher than Km. And so what that means is towards the end we see that the concentration of S is much, much higher than the value of Km. And so by the same logic that we used here, the sum of Km and the substrate concentration is about equal to simply the substrate concentration. And so if we take this mechanics methane equation it will simplify itself to this. So V knot is equal to V max divided by the ratio. | Michaelis menten Equation .txt |
And so by the same logic that we used here, the sum of Km and the substrate concentration is about equal to simply the substrate concentration. And so if we take this mechanics methane equation it will simplify itself to this. So V knot is equal to V max divided by the ratio. The denominator is approximately equal to this. And now these two quantities cancel out and we simply see that V Naught is equal to V max. So what that means is as we continually add concentration of as we continually increase the concentration of S, eventually our V knot will be the V max. | Michaelis menten Equation .txt |
The denominator is approximately equal to this. And now these two quantities cancel out and we simply see that V Naught is equal to V max. So what that means is as we continually add concentration of as we continually increase the concentration of S, eventually our V knot will be the V max. And once we reach the V max, it doesn't matter if we add more of that substrate. Adding more substrate will not have any effect on the rate of that enzyme catalyzed reaction. And that can be seen from this equation. | Michaelis menten Equation .txt |
And once we reach the V max, it doesn't matter if we add more of that substrate. Adding more substrate will not have any effect on the rate of that enzyme catalyzed reaction. And that can be seen from this equation. So v naught is equal to v max. V Naught is equal to V max is an equation that describes a rate law that has a 0th order. Remember, V is equal to K multiplied by the concentration to the 0th power. | Michaelis menten Equation .txt |
So v naught is equal to v max. V Naught is equal to V max is an equation that describes a rate law that has a 0th order. Remember, V is equal to K multiplied by the concentration to the 0th power. This is a zero Th order chemical reaction. And so what that means is this will cancel out because anything to the zero is one and so D equals K and V Naught is V and V max is the K value. And what that means is by changing the concentration, the substrate when we have a very high substrate concentration that will not affect the rate of that enzyme catalyzed reaction. | Michaelis menten Equation .txt |
This is a zero Th order chemical reaction. And so what that means is this will cancel out because anything to the zero is one and so D equals K and V Naught is V and V max is the K value. And what that means is by changing the concentration, the substrate when we have a very high substrate concentration that will not affect the rate of that enzyme catalyzed reaction. So once again, this tells us that the velocity approaches a maximum as the substrate concentration increases. And this describes a zero order reaction. This means that increasing the substrate concentration will not actually affect the rate of that chemical reaction when we're very far along the X axis to the right. | Michaelis menten Equation .txt |
So when we have low mass of ATP, we want to produce ATP. And so these are the enzyme, these are the allosteric effect, they're shown in blue that activate the process of glycolysis under low energy conditions. So in this particular case, if we have lots of Amp, the same Amp that inactivates this actually activates the phosphor fructose kinase. On top of that, the st fructose 26 bisphosphate that inactivates this actually activates this. So this molecule is activated by these two Alastairs effectors and pyruvate kinase is activated by the build up of fructose six bisphosphate. Now, why does that actually make sense? | Reciprocal Regulation of Gluconeogenesis and Glycolysis .txt |
On top of that, the st fructose 26 bisphosphate that inactivates this actually activates this. So this molecule is activated by these two Alastairs effectors and pyruvate kinase is activated by the build up of fructose six bisphosphate. Now, why does that actually make sense? Well, if these two molecules activate the activity of phosphorptokinase, we're going to basically create many more fructose one six bisphosphate. And as this molecule builds up in the concentration, it will depend on pyruvate kinase to transform these ultimately into pyruvate. And so to basically make sure we don't have a continual buildup of the fructose one six bisphosphate, it creates a positive feedback loop and the f 15 bisphosphate molecule actually activates that pyruvate kinase and that activates the process of glycolysis. | Reciprocal Regulation of Gluconeogenesis and Glycolysis .txt |
Well, if these two molecules activate the activity of phosphorptokinase, we're going to basically create many more fructose one six bisphosphate. And as this molecule builds up in the concentration, it will depend on pyruvate kinase to transform these ultimately into pyruvate. And so to basically make sure we don't have a continual buildup of the fructose one six bisphosphate, it creates a positive feedback loop and the f 15 bisphosphate molecule actually activates that pyruvate kinase and that activates the process of glycolysis. So let's summarize our results. So, when the cell has a low level of ATP relative to Amp, that means it basically has a low energy charge and it has a relatively high amount of Amp. And so what that means is we want to produce more of the ATP and we want to use less of the ATP. | Reciprocal Regulation of Gluconeogenesis and Glycolysis .txt |
So let's summarize our results. So, when the cell has a low level of ATP relative to Amp, that means it basically has a low energy charge and it has a relatively high amount of Amp. And so what that means is we want to produce more of the ATP and we want to use less of the ATP. So Gluconeogenesis is shut down, but Glycolysis is activated. And so we see that on the glycolytic pathway we have phosphorptokinase being activated by Amp and f 26 BP, while pyruvate kinase is activated by fructose one six bisphosphate. On the other hand, fructose one six bisphosphate is inactivated by these two molecules, amp and f 26 BP. | Reciprocal Regulation of Gluconeogenesis and Glycolysis .txt |
So Gluconeogenesis is shut down, but Glycolysis is activated. And so we see that on the glycolytic pathway we have phosphorptokinase being activated by Amp and f 26 BP, while pyruvate kinase is activated by fructose one six bisphosphate. On the other hand, fructose one six bisphosphate is inactivated by these two molecules, amp and f 26 BP. The pet carboxylates and the pyruvate carboxylates are both inactivated by ADP. And so we conclude that when ATP is plentiful in a cell, the gluconeogenic process gluconeogenesis predominates, while when ATP is scarce, glycolysis is the process that predominates. Now, one more thing I want to mention before we discuss how glucose affects these two processes in the next lecture is the following. | Reciprocal Regulation of Gluconeogenesis and Glycolysis .txt |
The pet carboxylates and the pyruvate carboxylates are both inactivated by ADP. And so we conclude that when ATP is plentiful in a cell, the gluconeogenic process gluconeogenesis predominates, while when ATP is scarce, glycolysis is the process that predominates. Now, one more thing I want to mention before we discuss how glucose affects these two processes in the next lecture is the following. Sometimes you'll hear that Latitude's principle basically dictates which one of these processes will actually take place. And that's not exactly right. We cannot use legit Lee's principle to explain why either this process takes place or the other process takes place. | Reciprocal Regulation of Gluconeogenesis and Glycolysis .txt |
Sometimes you'll hear that Latitude's principle basically dictates which one of these processes will actually take place. And that's not exactly right. We cannot use legit Lee's principle to explain why either this process takes place or the other process takes place. Why? Well, because legit Lee's principle is used strictly for those reactions which are at equilibrium. And if a reaction is at equilibrium, that means the gifts free energy in that process is zero. | Reciprocal Regulation of Gluconeogenesis and Glycolysis .txt |
Previously, we focused on the oxygen binding curve of myoglobin and hemoglobin. And we saw that in the case of myoglobin, myoglobin binds oxygen very strongly. It has a very high affinity for oxygen, and it binds oxygen in a noncooperative fashion. On the other hand, we saw that the shape for our hemoglobin curve was a sigmoidal shape. And this, this describes the cooperative behavior of hemoglobin. So even though hemoglobin has a lower affinity for oxygen than myoglobin, hemoglobin is able to bind oxygen in a cooperative fashion. | Hemoglobin vs Myoglobin as Oxygen Carrier .txt |
On the other hand, we saw that the shape for our hemoglobin curve was a sigmoidal shape. And this, this describes the cooperative behavior of hemoglobin. So even though hemoglobin has a lower affinity for oxygen than myoglobin, hemoglobin is able to bind oxygen in a cooperative fashion. And that's exactly why our body prefers to use hemoglobin as the carrier and the transport of oxygen inside our body. Now, that discussion was a more qualitative approach. Now let's take a look at a more quantitative approach as to why our body actually uses hemoglobin instead of myoglobin as the transporter and carrier of oxygen from the lungs to the tissues of our body. | Hemoglobin vs Myoglobin as Oxygen Carrier .txt |
And that's exactly why our body prefers to use hemoglobin as the carrier and the transport of oxygen inside our body. Now, that discussion was a more qualitative approach. Now let's take a look at a more quantitative approach as to why our body actually uses hemoglobin instead of myoglobin as the transporter and carrier of oxygen from the lungs to the tissues of our body. So let's begin by recalling some basic biological facts. Inside our lungs, the partial pressure of oxygen is about 100 mercury inside our resting tissue. When we're not exercising, the partial pressure drops to 40 mercury. | Hemoglobin vs Myoglobin as Oxygen Carrier .txt |
So let's begin by recalling some basic biological facts. Inside our lungs, the partial pressure of oxygen is about 100 mercury inside our resting tissue. When we're not exercising, the partial pressure drops to 40 mercury. And inside our exercising tissue, for example, if we're swimming or running, our partial pressure drops to about 20 mercury. So we want to use these values and the oxygen dissociation curves for myoglobin and hemoglobin to basically show why hemoglobin is a much better carrier of oxygen than myoglobin. So let's begin with the hemoglobin. | Hemoglobin vs Myoglobin as Oxygen Carrier .txt |
And inside our exercising tissue, for example, if we're swimming or running, our partial pressure drops to about 20 mercury. So we want to use these values and the oxygen dissociation curves for myoglobin and hemoglobin to basically show why hemoglobin is a much better carrier of oxygen than myoglobin. So let's begin with the hemoglobin. So this red curve describes the oxygen dissociation curve for hemoglobin. So as we go from right to left, from the lungs to our tissue, our hemoglobin essentially unloads and releases that oxygen. So let's begin inside our lungs. | Hemoglobin vs Myoglobin as Oxygen Carrier .txt |
So this red curve describes the oxygen dissociation curve for hemoglobin. So as we go from right to left, from the lungs to our tissue, our hemoglobin essentially unloads and releases that oxygen. So let's begin inside our lungs. And let's suppose we're going from the lungs to our resting tissue. So the lungs have a partial pressure of 100 mercury, and the corresponding Y value at this point is about zero 98. So that means about 98% of the hemoglobin is fully saturated inside our lungs. | Hemoglobin vs Myoglobin as Oxygen Carrier .txt |
And let's suppose we're going from the lungs to our resting tissue. So the lungs have a partial pressure of 100 mercury, and the corresponding Y value at this point is about zero 98. So that means about 98% of the hemoglobin is fully saturated inside our lungs. Now, when the hemoglobin travels down to our resting tissue, which is at a pressure of about 40 mercury, the corresponding Y value is about zero point 77. And that means about 77% of that hemoglobin is fully saturated with oxygen inside our resting tissue. Now, what that tells us is when the hemoglobin goes from the lungs to the resting tissue, there is a difference of about 21%. | Hemoglobin vs Myoglobin as Oxygen Carrier .txt |
Now, when the hemoglobin travels down to our resting tissue, which is at a pressure of about 40 mercury, the corresponding Y value is about zero point 77. And that means about 77% of that hemoglobin is fully saturated with oxygen inside our resting tissue. Now, what that tells us is when the hemoglobin goes from the lungs to the resting tissue, there is a difference of about 21%. And what that means is 21% of that oxygen of that hemoglobin has successfully unloaded and released the oxygen to the resting cells of our body. So this is how much oxygen can be unloaded by the hemoglobin when it goes from the lungs to the resting tissue. Now, what about if we're exercising? | Hemoglobin vs Myoglobin as Oxygen Carrier .txt |
And what that means is 21% of that oxygen of that hemoglobin has successfully unloaded and released the oxygen to the resting cells of our body. So this is how much oxygen can be unloaded by the hemoglobin when it goes from the lungs to the resting tissue. Now, what about if we're exercising? How much can hemoglobin deliver if our tissues are exercising? Well, in the case of the exercising tissue, the partial pressure is at 20 mercury. And we see that because we have this sigmoidal shape curve, there is a drastic drop in our fractional saturation of hemoglobin. | Hemoglobin vs Myoglobin as Oxygen Carrier .txt |
How much can hemoglobin deliver if our tissues are exercising? Well, in the case of the exercising tissue, the partial pressure is at 20 mercury. And we see that because we have this sigmoidal shape curve, there is a drastic drop in our fractional saturation of hemoglobin. So we go from here to about here. And this wide valley corresponds to about zero point 32. And that means when our tissue is exercising, 32% of that hemoglobin is fully saturated with oxygen. | Hemoglobin vs Myoglobin as Oxygen Carrier .txt |
So we go from here to about here. And this wide valley corresponds to about zero point 32. And that means when our tissue is exercising, 32% of that hemoglobin is fully saturated with oxygen. And so now, when we go from the lungs to our exercising tissue, there is a difference of 98% -32%. So 66% and that means 66% of the hemoglobin has unloaded and released that oxygen to the cells of our body that are exercising. And that is a lot of oxygen. | Hemoglobin vs Myoglobin as Oxygen Carrier .txt |
And so now, when we go from the lungs to our exercising tissue, there is a difference of 98% -32%. So 66% and that means 66% of the hemoglobin has unloaded and released that oxygen to the cells of our body that are exercising. And that is a lot of oxygen. And that means hemoglobin can successfully deliver the oxygen to our tissues of the body from the lungs. Now, what about myoglobin? Well, let's do the same exact thing for myoglobin. | Hemoglobin vs Myoglobin as Oxygen Carrier .txt |
And that means hemoglobin can successfully deliver the oxygen to our tissues of the body from the lungs. Now, what about myoglobin? Well, let's do the same exact thing for myoglobin. So in the case of myoglobin, so let's take out a marker. In the case of myoglobin, we begin once again at the lungs, just the same way we begin here at the lungs. So, at the lungs, we have 100 million meter of mercury and that corresponds to about 98% to zero. | Hemoglobin vs Myoglobin as Oxygen Carrier .txt |
So in the case of myoglobin, so let's take out a marker. In the case of myoglobin, we begin once again at the lungs, just the same way we begin here at the lungs. So, at the lungs, we have 100 million meter of mercury and that corresponds to about 98% to zero. 98 fractional saturation or 98% of the myoglobin is saturated in the lungs, which is the same value as for the hemoglobin case. But look what happens when we go down to this value which corresponds to the resting tissue. There is only a very, very small drop in a fractional saturation of myoglobin when we go from the lungs to the resting tissue, about 1% difference. | Hemoglobin vs Myoglobin as Oxygen Carrier .txt |
98 fractional saturation or 98% of the myoglobin is saturated in the lungs, which is the same value as for the hemoglobin case. But look what happens when we go down to this value which corresponds to the resting tissue. There is only a very, very small drop in a fractional saturation of myoglobin when we go from the lungs to the resting tissue, about 1% difference. And that means only about 1% of that myoglobin has successfully unloaded that oxygen into the tissue. And that's a very, very small amount. It's simply not enough for those cells in the resting tissue to actually use the oxygen to create enough ATP. | Hemoglobin vs Myoglobin as Oxygen Carrier .txt |
And that means only about 1% of that myoglobin has successfully unloaded that oxygen into the tissue. And that's a very, very small amount. It's simply not enough for those cells in the resting tissue to actually use the oxygen to create enough ATP. Now, if we examine the difference between the lungs and the exercising tissue, so going from the lungs to this point, this point corresponds to value of about zero point 91. So that means 91% of the myoglobin is saturated in exercising tissue of our body. And so 98 -91 gives us a difference of about 7% so this is a tremendous difference. | Hemoglobin vs Myoglobin as Oxygen Carrier .txt |
Now, if we examine the difference between the lungs and the exercising tissue, so going from the lungs to this point, this point corresponds to value of about zero point 91. So that means 91% of the myoglobin is saturated in exercising tissue of our body. And so 98 -91 gives us a difference of about 7% so this is a tremendous difference. 7% would not be enough for our body to actually create enough ATP molecules and to use the ATP molecules for the various processes. And that's precisely why it's the hemoglobin molecule and not the myoglobin that our body actually prefers as the carrier of oxygen, because it's the hemoglobin that can successfully unload enough oxygen. 21% in this case, and 66% in this case, to our cells of the body. | Hemoglobin vs Myoglobin as Oxygen Carrier .txt |
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