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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. Our myoglobin simply has too high of an affinity for oxygen and it will not be able to successfully unload enough oxygen to the resting tissue or to our exercising tissue. And that's exactly why it's myoglobin that is used as the storage protein that stores oxygen inside our muscle cells. But it's the hemoglobin that is used as the carrier, because it binds oxygen in a non cooperative fashion, which gives it a sigmoidal shape and it is able to successfully unload enough oxygen to the tissues of our body. | Hemoglobin vs Myoglobin as Oxygen Carrier .txt |
Our myoglobin simply has too high of an affinity for oxygen and it will not be able to successfully unload enough oxygen to the resting tissue or to our exercising tissue. And that's exactly why it's myoglobin that is used as the storage protein that stores oxygen inside our muscle cells. But it's the hemoglobin that is used as the carrier, because it binds oxygen in a non cooperative fashion, which gives it a sigmoidal shape and it is able to successfully unload enough oxygen to the tissues of our body. So once again, we see that hemoglobin's cooperative behavior allows it to unload much more oxygen successfully to the tissues than myoglobin. And this is why our body prefers to use hemoglobin as a transporter for oxygen inside our cardiovascular system, inside our bloodstream. And myoglobin simply has too high of an attraction to oxygen. | Hemoglobin vs Myoglobin as Oxygen Carrier .txt |
Now, where do we get our supply of acetylco enzyme A molecules? Well, we obtain it in the matrix of the mitochondria via processes such as the beta oxygen oxidation of fatty acids. We also generate acetylco enzyme A molecules via the decarboxylation of pyruvate, the catabolism of certain amino acids, as well as the breakdown of ketone bodies. But ultimately, this acetylco enzyme A molecule is found in the matrix of the mitochondria. And that poses a problem, because fatty acid synthesis takes place in the cytoplasm of the cell. But these acetylco enzyme A molecules are located in the matrix of the mitochondria. | Initiation of Fatty Acid Synthesis.txt |
But ultimately, this acetylco enzyme A molecule is found in the matrix of the mitochondria. And that poses a problem, because fatty acid synthesis takes place in the cytoplasm of the cell. But these acetylco enzyme A molecules are located in the matrix of the mitochondria. So we have to be able to move these acetylco enzyme A molecules from the matrix into the cytoplasm cell to actually initiate the process of fatty acid synthesis. Now, there's a problem with moving acetyl coenzyme A molecules across the membrane of the mitochondria. And the problem is it's water soluble. | Initiation of Fatty Acid Synthesis.txt |
So we have to be able to move these acetylco enzyme A molecules from the matrix into the cytoplasm cell to actually initiate the process of fatty acid synthesis. Now, there's a problem with moving acetyl coenzyme A molecules across the membrane of the mitochondria. And the problem is it's water soluble. So if we look at the acetyl coenzyme A molecule, the coenzyme a component of the acetyl coenzyme A molecule prevents that acetyl group from actually moving across the inner mitochondrial membrane. And so to ultimately allow the movement of that acetyl coenzyme A molecule across, we have to remove that coenzyme A. And so what happens is we transfer this CETL group onto oxalo acetate in the process that is catalyzed by citrate synthase to form the citrate molecule. | Initiation of Fatty Acid Synthesis.txt |
So if we look at the acetyl coenzyme A molecule, the coenzyme a component of the acetyl coenzyme A molecule prevents that acetyl group from actually moving across the inner mitochondrial membrane. And so to ultimately allow the movement of that acetyl coenzyme A molecule across, we have to remove that coenzyme A. And so what happens is we transfer this CETL group onto oxalo acetate in the process that is catalyzed by citrate synthase to form the citrate molecule. And now we can move that citrate across the inner and then the outer membrane of the mitochondria. And so this, if we recall, is simply the step number one in the citric acid cycle. Now, before we move on to the next steps of this process, actually moving it across the membrane of the mitochondria and then seeing what happens inside the cytoplasm, let's discuss which conditions actually lead to the synthesis of fatty acid. | Initiation of Fatty Acid Synthesis.txt |
And now we can move that citrate across the inner and then the outer membrane of the mitochondria. And so this, if we recall, is simply the step number one in the citric acid cycle. Now, before we move on to the next steps of this process, actually moving it across the membrane of the mitochondria and then seeing what happens inside the cytoplasm, let's discuss which conditions actually lead to the synthesis of fatty acid. So what conditions do we have to have in the matrix of the mitochondria to actually promote the process of fatty acid synthesis? So, in the matrix of the mitochondria, by the way, this is our matrix, our cytoplasm, the inner and the outer membrane of the mitochondria. So we know that in the matrix we have the citric acid cycle and electron transport chain basically generating ATP molecules. | Initiation of Fatty Acid Synthesis.txt |
So what conditions do we have to have in the matrix of the mitochondria to actually promote the process of fatty acid synthesis? So, in the matrix of the mitochondria, by the way, this is our matrix, our cytoplasm, the inner and the outer membrane of the mitochondria. So we know that in the matrix we have the citric acid cycle and electron transport chain basically generating ATP molecules. And so when we have high levels of ATP inside the matrix of the mitochondria, we don't want to actually produce any more ATP molecules. We want to stop the process of ATP synthesis. And so what happens is, when there are high levels of ATP in the matrix of mitochondria, that ATP act as an allosteric inhibitor of one of the enzymes of the citric acid cycle. | Initiation of Fatty Acid Synthesis.txt |
And so when we have high levels of ATP inside the matrix of the mitochondria, we don't want to actually produce any more ATP molecules. We want to stop the process of ATP synthesis. And so what happens is, when there are high levels of ATP in the matrix of mitochondria, that ATP act as an allosteric inhibitor of one of the enzymes of the citric acid cycle. So which enzyme? Isocytrade dehydrogenase. isocitric dehydrogenase basically transforms isocitrate into alpha ketoglutrate. | Initiation of Fatty Acid Synthesis.txt |
So which enzyme? Isocytrade dehydrogenase. isocitric dehydrogenase basically transforms isocitrate into alpha ketoglutrate. And when we have high levels of ATP, it blocks the activity of this enzyme and that leads to a build up of isocitrate in the matrix of the mitochondria. Now, isocitrate, if recalled back to the citric acid cycle, can be interconverted into citrate. So it basically converts back and forth. | Initiation of Fatty Acid Synthesis.txt |
And when we have high levels of ATP, it blocks the activity of this enzyme and that leads to a build up of isocitrate in the matrix of the mitochondria. Now, isocitrate, if recalled back to the citric acid cycle, can be interconverted into citrate. So it basically converts back and forth. But if we have high levels of isocitrate, we're also going to see an accumulation of citrate molecules and this will promote fatty acid synthesis. So high levels of ATP and high levels of citrate molecules basically stimulates the process of fatty acid synthesis. And that makes sense because we need ATP and we need citrate to actually begin the process of fatty acid synthesis. | Initiation of Fatty Acid Synthesis.txt |
But if we have high levels of isocitrate, we're also going to see an accumulation of citrate molecules and this will promote fatty acid synthesis. So high levels of ATP and high levels of citrate molecules basically stimulates the process of fatty acid synthesis. And that makes sense because we need ATP and we need citrate to actually begin the process of fatty acid synthesis. So once again, what actually promotes what stimulates fatty acid synthesis? Well, when the level of ATP in the matrix is high, this means that we no longer need to actually synthesize any more ATP. And therefore the ATP will create a negative feedback loop that will inhibit isocitrate dehydrogenase. | Initiation of Fatty Acid Synthesis.txt |
So once again, what actually promotes what stimulates fatty acid synthesis? Well, when the level of ATP in the matrix is high, this means that we no longer need to actually synthesize any more ATP. And therefore the ATP will create a negative feedback loop that will inhibit isocitrate dehydrogenase. And this causes a build up, is citrate, which in turn causes a build up of citrate molecules. And once we actually form citrate, which involves transferring acetyl, the Cetil group from acetyl co enzyme onto oxalacetate, then that citrate can actually move across the inner and the outer membrane of the mitochondria and into the cytoplasm of that cell. So in step three, we have citrate is then transported across the membrane and into the cytoplasm of that cell. | Initiation of Fatty Acid Synthesis.txt |
And this causes a build up, is citrate, which in turn causes a build up of citrate molecules. And once we actually form citrate, which involves transferring acetyl, the Cetil group from acetyl co enzyme onto oxalacetate, then that citrate can actually move across the inner and the outer membrane of the mitochondria and into the cytoplasm of that cell. So in step three, we have citrate is then transported across the membrane and into the cytoplasm of that cell. Now, the citrate itself is not actually used in the fatty acid synthesis process. We have to actually obtain that acetylcoanson a back. And so what happens is we have a process in which we take that citrate and we form back that oxylo acetate that we begin with. | Initiation of Fatty Acid Synthesis.txt |
Now, the citrate itself is not actually used in the fatty acid synthesis process. We have to actually obtain that acetylcoanson a back. And so what happens is we have a process in which we take that citrate and we form back that oxylo acetate that we begin with. And we also generate an acetyl co enzyme a molecule. And this is carried out by the enzyme we call ATP, citrate lyase. So in order to regenerate the CETL co enzyme a inside of plasma, the enzyme ATP Citrate Liaase, uses an ATP and a co enzyme to reform the acetyl coenzyme A and that oxalo acetate as the byproduct. | Initiation of Fatty Acid Synthesis.txt |
And we also generate an acetyl co enzyme a molecule. And this is carried out by the enzyme we call ATP, citrate lyase. So in order to regenerate the CETL co enzyme a inside of plasma, the enzyme ATP Citrate Liaase, uses an ATP and a co enzyme to reform the acetyl coenzyme A and that oxalo acetate as the byproduct. So this is the reaction shown here. So we have the citrate that is now on the cytoplasmic side, we have a coenzyme a that is different than the coenzyme a that we had here because remember, in this process, the coenzyme a was essentially kicked off. We combine these two by hydrolyzing ATP and we form an acetyl coenzyme a and the oxalo acetate a. | Initiation of Fatty Acid Synthesis.txt |
So this is the reaction shown here. So we have the citrate that is now on the cytoplasmic side, we have a coenzyme a that is different than the coenzyme a that we had here because remember, in this process, the coenzyme a was essentially kicked off. We combine these two by hydrolyzing ATP and we form an acetyl coenzyme a and the oxalo acetate a. So ultimately, what actually moved across the membranes of the mitochondria are the oxalo acetate and the Cecil group that was attached onto oxalo acetate. And it's the Cecil group that will ultimately be used to synthesize those fatty acids. So it's this acetyl coenzyme a that will now go on to help synthesize fatty acid molecules as we'll discuss in the next several lectures. | Initiation of Fatty Acid Synthesis.txt |
So ultimately, what actually moved across the membranes of the mitochondria are the oxalo acetate and the Cecil group that was attached onto oxalo acetate. And it's the Cecil group that will ultimately be used to synthesize those fatty acids. So it's this acetyl coenzyme a that will now go on to help synthesize fatty acid molecules as we'll discuss in the next several lectures. Now, what about this oxalo acetate? What is the fate of this oxylo acetate? Well, now we actually have to transform the oxalo acetate into a molecule that can move across the membrane back onto the matrix of the mitochondria so that we can recycle and reuse that oxylo acetate. | Initiation of Fatty Acid Synthesis.txt |
Now, what about this oxalo acetate? What is the fate of this oxylo acetate? Well, now we actually have to transform the oxalo acetate into a molecule that can move across the membrane back onto the matrix of the mitochondria so that we can recycle and reuse that oxylo acetate. The problem is, oxyloacetate cannot simply diffuse across the membrane of the mitochondria. And we have to transform that oxyloacetate in a two step process into pyruvate. So let's see how this actually takes place. | Initiation of Fatty Acid Synthesis.txt |
The problem is, oxyloacetate cannot simply diffuse across the membrane of the mitochondria. And we have to transform that oxyloacetate in a two step process into pyruvate. So let's see how this actually takes place. So we have oxalo acetate. We basically reduce oxylacetate by using the reduction power of NADH to form a malate. And this is step number five. | Initiation of Fatty Acid Synthesis.txt |
So we have oxalo acetate. We basically reduce oxylacetate by using the reduction power of NADH to form a malate. And this is step number five. So the oxalo acetate cannot cross the mitochondrial membrane. Therefore, to return back to the matrix, it is first transformed into malade by malade dehydrogenase. And this requires NADH. | Initiation of Fatty Acid Synthesis.txt |
So the oxalo acetate cannot cross the mitochondrial membrane. Therefore, to return back to the matrix, it is first transformed into malade by malade dehydrogenase. And this requires NADH. And so we produce NAD plus in this process. Now, once we form malade, an important process takes place that allows us not only to form the pyruvate that can now move across the matrix, across the membrane of the mitochondria, but we also generate NADPH and NADPH. And this is important, as we'll see in just a moment, because this is the NADPH that we're going to use in the fatty acid synthesis process. | Initiation of Fatty Acid Synthesis.txt |
And so we produce NAD plus in this process. Now, once we form malade, an important process takes place that allows us not only to form the pyruvate that can now move across the matrix, across the membrane of the mitochondria, but we also generate NADPH and NADPH. And this is important, as we'll see in just a moment, because this is the NADPH that we're going to use in the fatty acid synthesis process. So next, the malate undergoes an oxidative decorboxylation step that is catalyzed by the enzyme NADP plus linked malate enzyme, also known as malik enzyme. And this reaction is important because not only does it give us a way to actually move that molecule across the membrane of the mitochondria, it also generates that NADPH that will be used in fatty acid synthesis. So, malade in the presence of NADP plus and this enzyme, NADP plus linked malade enzyme, is transformed into pyruvate. | Initiation of Fatty Acid Synthesis.txt |
So next, the malate undergoes an oxidative decorboxylation step that is catalyzed by the enzyme NADP plus linked malate enzyme, also known as malik enzyme. And this reaction is important because not only does it give us a way to actually move that molecule across the membrane of the mitochondria, it also generates that NADPH that will be used in fatty acid synthesis. So, malade in the presence of NADP plus and this enzyme, NADP plus linked malade enzyme, is transformed into pyruvate. We essentially release the carbon dioxide and we form the NADPH. And it's this NADPH that will be used by fatty acid synthesis. In fact, this is the major pathway that produces the highest number of NADPH molecules that will be used by the fatty acid synthesis process. | Initiation of Fatty Acid Synthesis.txt |
We essentially release the carbon dioxide and we form the NADPH. And it's this NADPH that will be used by fatty acid synthesis. In fact, this is the major pathway that produces the highest number of NADPH molecules that will be used by the fatty acid synthesis process. The remaining Nadphs will be produced via the pentose phosphate pathway. Now, once we form pyruvate, it moves across the membranes of the mitochondria into the matrix. And inside the matrix, we use pyruvate carboxylase to transform the pyruvate into oxalo acetate. | Initiation of Fatty Acid Synthesis.txt |
Before the cells of our body, such as liver cells or skeleton muscle cells, can actually use their supply of glucose. They have to release the glucose from glycogen because inside our body we store glucose in the form we call glycogen. So the question that I would like to address in this lecture is how exactly do we break down glycogen inside the cells of our body? Well, glycogen, glycogen breakdown, also known as glycogen degradation, is the process by which we carry out three different steps to basically release the glucose molecule from glycogen. And this process actually involves four different enzymes, as we'll see in just a moment. So let's discuss the first step of glycogen breakdown. | Glycogen Breakdown .txt |
Well, glycogen, glycogen breakdown, also known as glycogen degradation, is the process by which we carry out three different steps to basically release the glucose molecule from glycogen. And this process actually involves four different enzymes, as we'll see in just a moment. So let's discuss the first step of glycogen breakdown. Now, the first step is known as phosphoralysis, and this process is catalyzed by an enzyme known as glycogen phosphorylase. Now, glycogen phosphorylase uses an orthophosphate molecule to actually cleave to break an alpha one four glycosytic bond between a terminal glucose molecule that contains a free hydroxyl group on the fourth carbon and the JSON glucose molecule. And this can be seen in the following picture. | Glycogen Breakdown .txt |
Now, the first step is known as phosphoralysis, and this process is catalyzed by an enzyme known as glycogen phosphorylase. Now, glycogen phosphorylase uses an orthophosphate molecule to actually cleave to break an alpha one four glycosytic bond between a terminal glucose molecule that contains a free hydroxyl group on the fourth carbon and the JSON glucose molecule. And this can be seen in the following picture. So we essentially have our first step of glycogen breakdown. So on the left side we have the reactant, the glycogen molecule that contains, let's suppose, N number of glucose molecules. And to simplify the diagram of only drawn two of these glucose molecules. | Glycogen Breakdown .txt |
So we essentially have our first step of glycogen breakdown. So on the left side we have the reactant, the glycogen molecule that contains, let's suppose, N number of glucose molecules. And to simplify the diagram of only drawn two of these glucose molecules. Now, this is the terminal glucose molecule that contains the free hydroxyl group on carbon number four of the glucose. And so this is the alpha one four glycocitic bond that will be cleaved by the glycogen phosphorlase. Now, the other reactant of this particular reaction is the orthophosphate. | Glycogen Breakdown .txt |
Now, this is the terminal glucose molecule that contains the free hydroxyl group on carbon number four of the glucose. And so this is the alpha one four glycocitic bond that will be cleaved by the glycogen phosphorlase. Now, the other reactant of this particular reaction is the orthophosphate. The orthophosphate actually acts as a nuclear file that cleaves this alpha one four glycocitic bond to basically form these two product molecules. We have a glucose one phosphate and we have the glycogen that now contains one less glucose because we removed this terminal glucose molecule here. Now we have this glycogen that contains N minus one number of glucose molecules. | Glycogen Breakdown .txt |
The orthophosphate actually acts as a nuclear file that cleaves this alpha one four glycocitic bond to basically form these two product molecules. We have a glucose one phosphate and we have the glycogen that now contains one less glucose because we removed this terminal glucose molecule here. Now we have this glycogen that contains N minus one number of glucose molecules. Now, inside the cells of our body, this reaction is a product favorite reaction and that's because of two important reasons. Number one is this reaction is energetically favorable. Why? | Glycogen Breakdown .txt |
Now, inside the cells of our body, this reaction is a product favorite reaction and that's because of two important reasons. Number one is this reaction is energetically favorable. Why? Well, recall that if we want to transform glucose into glucose one phosphate, we actually have to utilize and hydrolyze an ATP molecule. So normally if we want to transform glucose into glucose one phosphate, we have to use an ATP molecule. But let's see what happens in this particular reaction. | Glycogen Breakdown .txt |
Well, recall that if we want to transform glucose into glucose one phosphate, we actually have to utilize and hydrolyze an ATP molecule. So normally if we want to transform glucose into glucose one phosphate, we have to use an ATP molecule. But let's see what happens in this particular reaction. In this reaction we do release a glucose molecule, we take off the terminal glucose. In the process, we add up a spoil group without actually hydrolyzing an ATP molecule and this creates an energetically favorable process. So we essentially bypass the process of using an ATP molecule by releasing the glucose in the glucose one phosphate form. | Glycogen Breakdown .txt |
In this reaction we do release a glucose molecule, we take off the terminal glucose. In the process, we add up a spoil group without actually hydrolyzing an ATP molecule and this creates an energetically favorable process. So we essentially bypass the process of using an ATP molecule by releasing the glucose in the glucose one phosphate form. Now, the other reason why this reaction is product favorite is because inside our cells we generally have a much higher concentration of the orthophosphate reactive molecule than the glucose one phosphate product. In fact, the ratio of orthophosphate to this product is about 100 to one. And so because of that, because we have so much more of the reactants, that means that will drive this reaction toward the right side. | Glycogen Breakdown .txt |
Now, the other reason why this reaction is product favorite is because inside our cells we generally have a much higher concentration of the orthophosphate reactive molecule than the glucose one phosphate product. In fact, the ratio of orthophosphate to this product is about 100 to one. And so because of that, because we have so much more of the reactants, that means that will drive this reaction toward the right side. So this process, step one of glycogen breakdown, proceeds toward the right side, toward the product side. Because the cell contains a higher concentration of orthophosphate compared to glucose one phosphate, and because the formation of glucose one phosphate bypasses the usage of the ATP, it forms directly the glucose one phosphate from that glucose. And this is in fact energetically favorable. | Glycogen Breakdown .txt |
So this process, step one of glycogen breakdown, proceeds toward the right side, toward the product side. Because the cell contains a higher concentration of orthophosphate compared to glucose one phosphate, and because the formation of glucose one phosphate bypasses the usage of the ATP, it forms directly the glucose one phosphate from that glucose. And this is in fact energetically favorable. Now let's move on to step number two. So in step number two, what we ultimately want to do is, oh, and by the way, the glucose one phosphate that we form as a product in step one will actually be used in step three. But the glycogen and minus one is actually used in step two. | Glycogen Breakdown .txt |
Now let's move on to step number two. So in step number two, what we ultimately want to do is, oh, and by the way, the glucose one phosphate that we form as a product in step one will actually be used in step three. But the glycogen and minus one is actually used in step two. And what step two does is it restructures, it remodels the glycogen. It basically puts it into a form so that the glycogen phosphoralase can continue acting on it, cleaving it and releasing the glucose one phosphate molecule. So the reason for that is simple. | Glycogen Breakdown .txt |
And what step two does is it restructures, it remodels the glycogen. It basically puts it into a form so that the glycogen phosphoralase can continue acting on it, cleaving it and releasing the glucose one phosphate molecule. So the reason for that is simple. The glycogen phosphorase is limited to what it can actually do. The glycogen phosphorolase can only cleave alpha one four glycocitic bonds. It cannot cleave alpha one six glycocitic bonds. | Glycogen Breakdown .txt |
The glycogen phosphorase is limited to what it can actually do. The glycogen phosphorolase can only cleave alpha one four glycocitic bonds. It cannot cleave alpha one six glycocitic bonds. In fact, it stops cleaving the alpha one four glycocitic bonds for residues for glucose molecules away from the branching point, the nearest alpha one six glycocitic bond. So glycogen phosphoralase, the enzyme that catalyzes step one of glycogen breakdown, can only cleave alpha one four glycocitic bonds. It does not cleave alpha one six glycocitic bonds that are found in glycogen. | Glycogen Breakdown .txt |
In fact, it stops cleaving the alpha one four glycocitic bonds for residues for glucose molecules away from the branching point, the nearest alpha one six glycocitic bond. So glycogen phosphoralase, the enzyme that catalyzes step one of glycogen breakdown, can only cleave alpha one four glycocitic bonds. It does not cleave alpha one six glycocitic bonds that are found in glycogen. In fact, this enzyme stops four residues away from the nearest branching point. And we'll talk more about that in this particular diagram. Now, step number two can actually be broken down into two different steps and that's because step number two utilizes two different types of enzymes. | Glycogen Breakdown .txt |
In fact, this enzyme stops four residues away from the nearest branching point. And we'll talk more about that in this particular diagram. Now, step number two can actually be broken down into two different steps and that's because step number two utilizes two different types of enzymes. One of these enzymes is known as transferase and the other enzyme is known as alpha 13 glucosidase. Now, in eukaryotic cells, these two enzymes are actually found on a single enzyme. So in eukaryotic cells we have this single bifunctional enzyme that contains these two different types of enzymes, transferase and alpha 116 glucosedase, these two different types of catalytic sites that basically catalyze two different types of reactions. | Glycogen Breakdown .txt |
One of these enzymes is known as transferase and the other enzyme is known as alpha 13 glucosidase. Now, in eukaryotic cells, these two enzymes are actually found on a single enzyme. So in eukaryotic cells we have this single bifunctional enzyme that contains these two different types of enzymes, transferase and alpha 116 glucosedase, these two different types of catalytic sites that basically catalyze two different types of reactions. So let's begin by examining transferase and what it actually does. So suppose we have the following glycogen molecules. So it's a simple molecule with a single alpha one six glycocitic bond. | Glycogen Breakdown .txt |
So let's begin by examining transferase and what it actually does. So suppose we have the following glycogen molecules. So it's a simple molecule with a single alpha one six glycocitic bond. So these bonds here are the alpha one four glycocitic bonds and this bond here is the alpha one six glycocitic bond. Now remember what I said about glycogen phosphorase. It can only cleave alpha one four glycocitic bonds and it stops cleaving the alpha one four glycocitic bonds when it gets to four residues away from the nearest branching point. | Glycogen Breakdown .txt |
So these bonds here are the alpha one four glycocitic bonds and this bond here is the alpha one six glycocitic bond. Now remember what I said about glycogen phosphorase. It can only cleave alpha one four glycocitic bonds and it stops cleaving the alpha one four glycocitic bonds when it gets to four residues away from the nearest branching point. The nearest alpha one six glycocitic bonds. So on this particular section, we have 1234 glucose residues. And so the glycogen phosphorase will no longer be able to cleave these alpha one four glycocity bonds because it's only four away from this branching point. | Glycogen Breakdown .txt |
The nearest alpha one six glycocitic bonds. So on this particular section, we have 1234 glucose residues. And so the glycogen phosphorase will no longer be able to cleave these alpha one four glycocity bonds because it's only four away from this branching point. And so to fix that problem, what transferase does is it takes this region of three residues away from this section and moves it shifts us onto this region here. So it basically forms the following product. So it removes this and extends this linear section by three glucose molecules. | Glycogen Breakdown .txt |
And so to fix that problem, what transferase does is it takes this region of three residues away from this section and moves it shifts us onto this region here. So it basically forms the following product. So it removes this and extends this linear section by three glucose molecules. So transphrase catalyzes the shift of three glucose residues from one branch, this branch, to the other branch, this branch here. And this process basically leaves a single glucose molecule that is attached to this entire region by an alpha one six glycocitic bond. Now, this is where alpha one six glucosidase actually comes into place, comes into play, because what this enzyme does is it is able to cleave that alpha one six glycocitic bond. | Glycogen Breakdown .txt |
So transphrase catalyzes the shift of three glucose residues from one branch, this branch, to the other branch, this branch here. And this process basically leaves a single glucose molecule that is attached to this entire region by an alpha one six glycocitic bond. Now, this is where alpha one six glucosidase actually comes into place, comes into play, because what this enzyme does is it is able to cleave that alpha one six glycocitic bond. So the alpha one six glucosidase cleaves this alpha one six glycocitic bond and releases this free glucose. And that free glucose is then transformed by hexokinase to form the glucose one phosphate, which then goes on to step three, as we'll see in just in a moment. And we also form this product. | Glycogen Breakdown .txt |
So the alpha one six glucosidase cleaves this alpha one six glycocitic bond and releases this free glucose. And that free glucose is then transformed by hexokinase to form the glucose one phosphate, which then goes on to step three, as we'll see in just in a moment. And we also form this product. Now, notice that when we go from this molecule to this molecule, we essentially remove the branching points. We basically transform the branched polymer of glycogen to a linear polymer of glycogen. And now this only contains the alpha 114 glycosytic bonds that can be cleaved by glycogen phosphorase. | Glycogen Breakdown .txt |
Now, notice that when we go from this molecule to this molecule, we essentially remove the branching points. We basically transform the branched polymer of glycogen to a linear polymer of glycogen. And now this only contains the alpha 114 glycosytic bonds that can be cleaved by glycogen phosphorase. And so once we form this linear glycogen in step two, the glycogen phosphorase moves on to this glycogen and begins breaking these alpha one four glycocitic bonds and those glucose one phosphate molecules produce, then go on to step three. And so let's move on to step three and let's see what happens in step three. Now in step three, we basically transform the glucose one phosphate into glucose six phosphate. | Glycogen Breakdown .txt |
And so once we form this linear glycogen in step two, the glycogen phosphorase moves on to this glycogen and begins breaking these alpha one four glycocitic bonds and those glucose one phosphate molecules produce, then go on to step three. And so let's move on to step three and let's see what happens in step three. Now in step three, we basically transform the glucose one phosphate into glucose six phosphate. The reason we need to do that is because the glucose six phosphate can go on to basically react in different types of pathways. For instance, in skeleton muscle cells, the glucose six phosphate can undergo glycolysis to form ATP. In liver cells, the glucose six phosphate can be transformed into glucose and then released into the blood to help regulate the blood plasma, the glucose blood plasma concentration and so forth. | Glycogen Breakdown .txt |
The reason we need to do that is because the glucose six phosphate can go on to basically react in different types of pathways. For instance, in skeleton muscle cells, the glucose six phosphate can undergo glycolysis to form ATP. In liver cells, the glucose six phosphate can be transformed into glucose and then released into the blood to help regulate the blood plasma, the glucose blood plasma concentration and so forth. Now, the enzyme that catalyzes step three is phosphoglucom mutates. Remember that a mutase basically transfers a group from one location to a different location on that same molecule. So what phosphorluca mutase actually does is it transfers that phosphoryl group from carbon number one to carbon number six. | Glycogen Breakdown .txt |
Now, the enzyme that catalyzes step three is phosphoglucom mutates. Remember that a mutase basically transfers a group from one location to a different location on that same molecule. So what phosphorluca mutase actually does is it transfers that phosphoryl group from carbon number one to carbon number six. Now we begin with glucose one phosphate and we end with glucose six phosphate. But what we actually don't show in this diagram is that we actually have an intermediate molecule involved and that intermediate molecule is glucose 116 bisphosphate. So if we examine the active side of this enzyme, phosphogluca mutase, we're going to see a modified serine residue. | Glycogen Breakdown .txt |
Now we begin with glucose one phosphate and we end with glucose six phosphate. But what we actually don't show in this diagram is that we actually have an intermediate molecule involved and that intermediate molecule is glucose 116 bisphosphate. So if we examine the active side of this enzyme, phosphogluca mutase, we're going to see a modified serine residue. And that Serene residue actually plays a catalytic role of catalyzing this reaction. So inside the active side of this enzyme, we have a serine that has been modified. We attached a phosphoryl group onto that Serene. | Glycogen Breakdown .txt |
And that Serene residue actually plays a catalytic role of catalyzing this reaction. So inside the active side of this enzyme, we have a serine that has been modified. We attached a phosphoryl group onto that Serene. So before this reaction actually begins, that serine contains the phosphoryl group. And so when this reaction takes place, that phosphoryl group is transferred from the Serene residue onto carbon six of this glucose, forming that glucose one six bisphosphate intermediate. Now, in the next step of this process, this phosphoryl group is transferred from carbon one onto so from carbon one of the glucose 116 bisphosphate onto that Serene residue. | Glycogen Breakdown .txt |
So before this reaction actually begins, that serine contains the phosphoryl group. And so when this reaction takes place, that phosphoryl group is transferred from the Serene residue onto carbon six of this glucose, forming that glucose one six bisphosphate intermediate. Now, in the next step of this process, this phosphoryl group is transferred from carbon one onto so from carbon one of the glucose 116 bisphosphate onto that Serene residue. And what that does is it regenerates the active side of this phosphoglucomutase enzyme and it forms that glucose six phosphate. So we see that glycogen breakdown. Glycogen degradation consists of three major steps and involves four major enzymes. | Glycogen Breakdown .txt |
And what that does is it regenerates the active side of this phosphoglucomutase enzyme and it forms that glucose six phosphate. So we see that glycogen breakdown. Glycogen degradation consists of three major steps and involves four major enzymes. In step one, the entire goal is to release that glucose in the glucose one phosphate form. In step two, the entire goal is to remodel restructure that glycogen so that the glycogen phosphorlase could actually continue breaking down the glycogen and releasing those glucose one phosphate molecules. And in step three, the entire goal is to transform all those glucose one phosphate molecules into a form, namely glucose six phosphate. | Glycogen Breakdown .txt |
The next topic in our study of biochemistry is enzyme. So what exactly is an enzyme? What's the purpose of enzymes? And what are some facts that you have to know about enzymes in general? So this is what we're going to discuss in this lecture. So an enzyme is basically a biological molecule with remarkable capabilities. | Properties of Enzymes .txt |
And what are some facts that you have to know about enzymes in general? So this is what we're going to discuss in this lecture. So an enzyme is basically a biological molecule with remarkable capabilities. What they do is they catalyze all of their different types of biological processes and reactions that take place inside our cells. And without the enzymes catalyzing the reactions, cellular processes would essentially hold to a rate that would make life impossible, at least in the way that we know life today. So the first thing you have to know about enzymes is an enzyme is a biological molecule that catalyzes speeds up the rate of reactions. | Properties of Enzymes .txt |
What they do is they catalyze all of their different types of biological processes and reactions that take place inside our cells. And without the enzymes catalyzing the reactions, cellular processes would essentially hold to a rate that would make life impossible, at least in the way that we know life today. So the first thing you have to know about enzymes is an enzyme is a biological molecule that catalyzes speeds up the rate of reactions. Now, in our discussion on hemorrglobin, we mentioned one important enzyme, namely carbonic anhydrase. And we said that it was carbonic anhydrase that essentially speeds up and allows the conversion of carbon dioxide into its polar form, namely bicarbonate ions. And this is exactly what allows us to actually store the carbon dioxide inside our blood plasma. | Properties of Enzymes .txt |
Now, in our discussion on hemorrglobin, we mentioned one important enzyme, namely carbonic anhydrase. And we said that it was carbonic anhydrase that essentially speeds up and allows the conversion of carbon dioxide into its polar form, namely bicarbonate ions. And this is exactly what allows us to actually store the carbon dioxide inside our blood plasma. So carbonic anhydrates essentially hydrates. So it combines carbon dioxide with water to produce carbonic acid. And carbonic acid, being a relatively strong acid, will dissociate into these two polar ions, hydrogen ions and bicarbonate ions. | Properties of Enzymes .txt |
So carbonic anhydrates essentially hydrates. So it combines carbon dioxide with water to produce carbonic acid. And carbonic acid, being a relatively strong acid, will dissociate into these two polar ions, hydrogen ions and bicarbonate ions. Now, carbonic anhydrates is a very efficient, very effective enzyme, like most enzymes are. In fact, this molecule can convert. The enzyme can transform 1 million of these carbon dioxide molecules every single second. | Properties of Enzymes .txt |
Now, carbonic anhydrates is a very efficient, very effective enzyme, like most enzymes are. In fact, this molecule can convert. The enzyme can transform 1 million of these carbon dioxide molecules every single second. So it increases the rate by 1 million compared to its uncategorized form. So this enzyme basically helps us transform the non polar carbon dioxide that cannot dissolve inside our blood into a form that can be dissolved inside our blood. And that's precisely what allows us to effectively and quickly get rid of the carbon dioxide from the cells and eventually expelled by the lungs of our body. | Properties of Enzymes .txt |
So it increases the rate by 1 million compared to its uncategorized form. So this enzyme basically helps us transform the non polar carbon dioxide that cannot dissolve inside our blood into a form that can be dissolved inside our blood. And that's precisely what allows us to effectively and quickly get rid of the carbon dioxide from the cells and eventually expelled by the lungs of our body. Now, fact number two about enzymes. Enzymes typically transform one form of energy into a much more useful form of energy. And one example is the process of photosynthesis, which takes place in plants. | Properties of Enzymes .txt |
Now, fact number two about enzymes. Enzymes typically transform one form of energy into a much more useful form of energy. And one example is the process of photosynthesis, which takes place in plants. So inside plants, we have a variety of different types of enzymes that essentially transform. They harvest or capture the energy that is stored in electromagnetic radiation that comes from the sun, namely light. So they transform the energy that is stored in light into energy stored in the chemical bonds of glucose and sugar molecules. | Properties of Enzymes .txt |
So inside plants, we have a variety of different types of enzymes that essentially transform. They harvest or capture the energy that is stored in electromagnetic radiation that comes from the sun, namely light. So they transform the energy that is stored in light into energy stored in the chemical bonds of glucose and sugar molecules. Now, humans and other animals then eat that glucose, and they themselves use enzymes in the process we're going to discuss eventually the process is glycolysis, Pyruvate decarboxylation, and then the Krebs cycle. So basically, in these processes, we have many different enzymes that essentially catalyze the transformation of the energy stored in the chemical bonds of glucose into the energy that is stored in the proton gradient that exists across the membrane of mitochondria and then the energy stored in that membrane in the electrochemical gradient due to the protons found across the mitochondrial membrane. That energy transformed into energy stored in the bonds of ATP molecules adenosine triphosphates. | Properties of Enzymes .txt |
Now, humans and other animals then eat that glucose, and they themselves use enzymes in the process we're going to discuss eventually the process is glycolysis, Pyruvate decarboxylation, and then the Krebs cycle. So basically, in these processes, we have many different enzymes that essentially catalyze the transformation of the energy stored in the chemical bonds of glucose into the energy that is stored in the proton gradient that exists across the membrane of mitochondria and then the energy stored in that membrane in the electrochemical gradient due to the protons found across the mitochondrial membrane. That energy transformed into energy stored in the bonds of ATP molecules adenosine triphosphates. And we'll discuss that in much more detail eventually. So we see that these enzymes are very, very good at transforming one form of energy that we can't use into a form that we can use, and that is what enzymes do. Number three enzymes typically do not act alone, and they require additional molecules. | Properties of Enzymes .txt |
And we'll discuss that in much more detail eventually. So we see that these enzymes are very, very good at transforming one form of energy that we can't use into a form that we can use, and that is what enzymes do. Number three enzymes typically do not act alone, and they require additional molecules. And these molecules are known as Cofactors. So Cofactors are helping molecules that are needed for the enzymes to actually function effectively and efficiently. So when an enzyme is not bound to its Cofactor, we call the enzyme apoenzyme. | Properties of Enzymes .txt |
And these molecules are known as Cofactors. So Cofactors are helping molecules that are needed for the enzymes to actually function effectively and efficiently. So when an enzyme is not bound to its Cofactor, we call the enzyme apoenzyme. But when the Cofactor is bound to the APO enzyme, we call that a hollow enzyme. So the hollow enzyme is simply an enzyme bound to its Cofactor. Now, we have many, many different types of Cofactors, as we'll eventually see. | Properties of Enzymes .txt |
But when the Cofactor is bound to the APO enzyme, we call that a hollow enzyme. So the hollow enzyme is simply an enzyme bound to its Cofactor. Now, we have many, many different types of Cofactors, as we'll eventually see. But we can categorize Cofactors into two groups, into two categories. We have metal ions and we also have organic molecules known as coenzymes that are usually formed from vitamins. Now, one example of a metal ion that acts as a cofactor for carbonic and hydrates is the zinc atom. | Properties of Enzymes .txt |
But we can categorize Cofactors into two groups, into two categories. We have metal ions and we also have organic molecules known as coenzymes that are usually formed from vitamins. Now, one example of a metal ion that acts as a cofactor for carbonic and hydrates is the zinc atom. And we'll talk about that in detail in a future electra. Now, coenzymes can bind onto proteins either strongly or weakly. And if we have a coenzyme that is bound very tightly to the enzyme that is known as a prosthetic group number four enzymes are extremely efficient and extremely specific molecules. | Properties of Enzymes .txt |
And we'll talk about that in detail in a future electra. Now, coenzymes can bind onto proteins either strongly or weakly. And if we have a coenzyme that is bound very tightly to the enzyme that is known as a prosthetic group number four enzymes are extremely efficient and extremely specific molecules. And what that means is enzymes only bind to specific substrate specific molecules and they carry out either a single reaction or a set of reactions that are closely related to one another. So enzymes bind to specific reactants. We also call substrates and catalyze a single reaction or a set of related reactions. | Properties of Enzymes .txt |
And what that means is enzymes only bind to specific substrate specific molecules and they carry out either a single reaction or a set of reactions that are closely related to one another. So enzymes bind to specific reactants. We also call substrates and catalyze a single reaction or a set of related reactions. And enzymes are highly efficient and limit the number of unwanted products. So, for example, in the case of carbonic and hydrates, carbonic and hydrates binds the CO2 and the water, and the CO2 is the substrate. Now, CO2 can react with water in many different ways. | Properties of Enzymes .txt |
And enzymes are highly efficient and limit the number of unwanted products. So, for example, in the case of carbonic and hydrates, carbonic and hydrates binds the CO2 and the water, and the CO2 is the substrate. Now, CO2 can react with water in many different ways. For example, in this particular case, we saw that we can produce sugar molecules and oxygen molecules. And these are unwanted products, at least in this particular case. So what carbonic and hydrase does is it ensures that we form only a single type of product. | Properties of Enzymes .txt |
For example, in this particular case, we saw that we can produce sugar molecules and oxygen molecules. And these are unwanted products, at least in this particular case. So what carbonic and hydrase does is it ensures that we form only a single type of product. We do not form any unwanted products in our reaction. So enzymes are highly specific. Another example of a highly specific enzyme that carries out a set of related reactions is tryptin. | Properties of Enzymes .txt |
We do not form any unwanted products in our reaction. So enzymes are highly specific. Another example of a highly specific enzyme that carries out a set of related reactions is tryptin. So Trypsin is found in our digestive system. It's a digestive enzyme. And what it does is it binds to polypeptides, to proteins that we ingest into our body. | Properties of Enzymes .txt |
So Trypsin is found in our digestive system. It's a digestive enzyme. And what it does is it binds to polypeptides, to proteins that we ingest into our body. And it basically carries out a set of two closely related reactions. In one of the reactions, it basically cleaves peptide bonds on the carboxyl side of lysine. In the other reaction, it binds and cleaves. | Properties of Enzymes .txt |
And it basically carries out a set of two closely related reactions. In one of the reactions, it basically cleaves peptide bonds on the carboxyl side of lysine. In the other reaction, it binds and cleaves. On the carboxyl side of the arginine amino acid so this trypsin has a single type of has a single type of substrate, namely the polypeptide and it carries out two sets, two types of very similar reactions in one reaction and Cleaves lysine on the carboxyl side in the other reaction cleaves Arginine on the carboxyl side. Now, number five nearly all enzymes are proteins. So long ago we essentially thought that all enzymes were proteins. | Properties of Enzymes .txt |
On the carboxyl side of the arginine amino acid so this trypsin has a single type of has a single type of substrate, namely the polypeptide and it carries out two sets, two types of very similar reactions in one reaction and Cleaves lysine on the carboxyl side in the other reaction cleaves Arginine on the carboxyl side. Now, number five nearly all enzymes are proteins. So long ago we essentially thought that all enzymes were proteins. But now we know that some enzymes are actually RNA molecules. So RNA molecules, certain RNA molecules also have the ability to catalyze reactions as we'll see eventually. And the last thing we're going to mention about enzymes is enzymes are not actually used up or not depleted in chemical reactions. | Properties of Enzymes .txt |
But now we know that some enzymes are actually RNA molecules. So RNA molecules, certain RNA molecules also have the ability to catalyze reactions as we'll see eventually. And the last thing we're going to mention about enzymes is enzymes are not actually used up or not depleted in chemical reactions. And if enzymes are changed or altered in some way in the reaction at the end of that reaction the enzyme will assume its original shape and original structure. So enzymes are not used up and remain unchanged at the end of the reaction. Now, this is not to say that enzymes during the reaction are unchanged in some way. | Properties of Enzymes .txt |
And if enzymes are changed or altered in some way in the reaction at the end of that reaction the enzyme will assume its original shape and original structure. So enzymes are not used up and remain unchanged at the end of the reaction. Now, this is not to say that enzymes during the reaction are unchanged in some way. They might be changed, their structure might be changed. But at the end of the reaction when the enzyme releases the substrate it assumes its original structure and its original shape. So these are the six facts you have to remember about enzymes. | Properties of Enzymes .txt |
They might be changed, their structure might be changed. But at the end of the reaction when the enzyme releases the substrate it assumes its original structure and its original shape. So these are the six facts you have to remember about enzymes. Enzymes greatly increase the rate at which reactions take place. Enzymes typically help transform one form of energy into much useful form of energy. Three enzymes do not function alone and they typically do not. | Properties of Enzymes .txt |
Enzymes greatly increase the rate at which reactions take place. Enzymes typically help transform one form of energy into much useful form of energy. Three enzymes do not function alone and they typically do not. And they typically need these helper. Molecules we call cofactors. Number four enzymes are highly specific. | Properties of Enzymes .txt |
And they typically need these helper. Molecules we call cofactors. Number four enzymes are highly specific. They bind specific substrates and carry out only a single reaction or a set of reactions that are similar as we saw in the case of trypsin number five nearly all enzymes are proteins. Some enzymes are RNA molecules. And number six enzymes are not depleted. | Properties of Enzymes .txt |
So so far we discussed pedigrees that describe diseases that are sex link recessive. We also looked at those pedigrees that describe autosomal recessive traits. Now let's take a look at the following pedigree that will describe autosomal dominant traits. So what we want to basically show in this lecture is that whatever the disease is that is described by this pedigree, it cannot be sex linked dominant and it cannot be sex link recessive. And we want to show that this could be autosomal dominant. So show that a disease described by the following pedigree cannot be sex link recessive and sex linked dominant. | Pedigree Analysis for Autosomal Dominant Traits .txt |
So what we want to basically show in this lecture is that whatever the disease is that is described by this pedigree, it cannot be sex linked dominant and it cannot be sex link recessive. And we want to show that this could be autosomal dominant. So show that a disease described by the following pedigree cannot be sex link recessive and sex linked dominant. So as always, to show that it's not something, we have to begin by assuming that it is that. So let's begin by assuming that it is sex length. Let's say recessive. | Pedigree Analysis for Autosomal Dominant Traits .txt |
So as always, to show that it's not something, we have to begin by assuming that it is that. So let's begin by assuming that it is sex length. Let's say recessive. So it's sex length recessive. And what that basically means is we have an x uppercase B that basically describes the normal gene, and then we have the x lowercase B that describes the gene for that disease. Okay? | Pedigree Analysis for Autosomal Dominant Traits .txt |
So it's sex length recessive. And what that basically means is we have an x uppercase B that basically describes the normal gene, and then we have the x lowercase B that describes the gene for that disease. Okay? So if this were true, if it is sex link recessive, then what that means is this female individual must be x lowercase b, x lowercase B and this individual, because it's a male and it's normal, that means we must have x uppercase B and y. So let's actually carry out the following crossing process between these two individuals and let's discuss what the distribution is of the genotypes of the offspring produce. And let's see if that's consistent with information given to us in this pedigree. | Pedigree Analysis for Autosomal Dominant Traits .txt |
So if this were true, if it is sex link recessive, then what that means is this female individual must be x lowercase b, x lowercase B and this individual, because it's a male and it's normal, that means we must have x uppercase B and y. So let's actually carry out the following crossing process between these two individuals and let's discuss what the distribution is of the genotypes of the offspring produce. And let's see if that's consistent with information given to us in this pedigree. So remember, this is generation one, these are the individuals of generation two, and these are the individuals of generation three. So we have, this individual produces either this sperm cell or this sperm cell. This produces only one type of xcel, x lowercase B. | Pedigree Analysis for Autosomal Dominant Traits .txt |
So remember, this is generation one, these are the individuals of generation two, and these are the individuals of generation three. So we have, this individual produces either this sperm cell or this sperm cell. This produces only one type of xcel, x lowercase B. So let's continue this punitive square. So we basically have x uppercase b, x lowercase b. We have x uppercase b, x lowercase b. | Pedigree Analysis for Autosomal Dominant Traits .txt |
So let's continue this punitive square. So we basically have x uppercase b, x lowercase b. We have x uppercase b, x lowercase b. We have x uppercase by, x uppercase by. Now notice what this punning square is telling us. It tells us that 100% of the offspring that are produced, the male offspring, so this one and this one must actually exhibit that particular disease phenotype, because we have x lowercase by and x lowercase by. | Pedigree Analysis for Autosomal Dominant Traits .txt |
We have x uppercase by, x uppercase by. Now notice what this punning square is telling us. It tells us that 100% of the offspring that are produced, the male offspring, so this one and this one must actually exhibit that particular disease phenotype, because we have x lowercase by and x lowercase by. Now that is consistent with this individual because this individual must be x lowercase by to actually display that disease phenotype. But this individual does not display that phenotype, it is male. So that means it must be x uppercase by. | Pedigree Analysis for Autosomal Dominant Traits .txt |
Now that is consistent with this individual because this individual must be x lowercase by to actually display that disease phenotype. But this individual does not display that phenotype, it is male. So that means it must be x uppercase by. And this genotype cannot exist if we cross these two individuals as shown in the following pundit square. And so what that means is this pedigree cannot describe a disease that is sex link recessive. So it can't be sex link recessive as a result of this inconsistency between the pedigree analysis and the pun and square analysis. | Pedigree Analysis for Autosomal Dominant Traits .txt |
And this genotype cannot exist if we cross these two individuals as shown in the following pundit square. And so what that means is this pedigree cannot describe a disease that is sex link recessive. So it can't be sex link recessive as a result of this inconsistency between the pedigree analysis and the pun and square analysis. So let's continue and let's move on to the sex length dominant and let's show that this cannot be sex length dominant, so it can't be this. So let's put an X over A. What about B? | Pedigree Analysis for Autosomal Dominant Traits .txt |
So let's continue and let's move on to the sex length dominant and let's show that this cannot be sex length dominant, so it can't be this. So let's put an X over A. What about B? Now let's assume that it's sex linked dominant. Can it be sex linked dominant? Well, if it's sex linked dominant, what that means is this individual, so this individual will have the disease, will have the phenotype for that disease, this individual will have the phenotype for that disease. | Pedigree Analysis for Autosomal Dominant Traits .txt |
Now let's assume that it's sex linked dominant. Can it be sex linked dominant? Well, if it's sex linked dominant, what that means is this individual, so this individual will have the disease, will have the phenotype for that disease, this individual will have the phenotype for that disease. And it also means that this individual will also have the disease for that particular phenotype for that particular disease, all other individuals. So we have X lowercase by and X lowercase BX lowercase B, these individuals will be normal. So with this in mind, let's fill out the following pedigree. | Pedigree Analysis for Autosomal Dominant Traits .txt |
And it also means that this individual will also have the disease for that particular phenotype for that particular disease, all other individuals. So we have X lowercase by and X lowercase BX lowercase B, these individuals will be normal. So with this in mind, let's fill out the following pedigree. So we have a male that is normal, and the only time that a male is normal is this, right over here. So we have X lowercase B and Y. And here we also have a normal male. | Pedigree Analysis for Autosomal Dominant Traits .txt |
So we have a male that is normal, and the only time that a male is normal is this, right over here. So we have X lowercase B and Y. And here we also have a normal male. So this must be X lowercase by. This by the same reasoning, must be X lowercase by, and this must be X lowercase B Y. This must be X lowercase B and Y. | Pedigree Analysis for Autosomal Dominant Traits .txt |
So this must be X lowercase by. This by the same reasoning, must be X lowercase by, and this must be X lowercase B Y. This must be X lowercase B and Y. The only time that a female is normal is when they have this particular genotype. So we have a normal female here, that means we have X lowercase by, x lowercase by. This is a normal female as well. | Pedigree Analysis for Autosomal Dominant Traits .txt |
The only time that a female is normal is when they have this particular genotype. So we have a normal female here, that means we have X lowercase by, x lowercase by. This is a normal female as well. This is a normal female and this is a normal female. Okay. And then we have the other one. | Pedigree Analysis for Autosomal Dominant Traits .txt |
This is a normal female and this is a normal female. Okay. And then we have the other one. So here we have a male that carries, that, has that phenotype or that disease. So that means it's uppercase B and Y. This one must also be X uppercase B and Y. | Pedigree Analysis for Autosomal Dominant Traits .txt |
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