 How a new set up for everyone, not for you, because you started the class na yesterday, so hopefully things will go smoothly with regards to my internet since I am having two Google Meet open today and presenting into two, then recording in one. So again, good morning to everyone, so welcome to the finals of clinical chemistry one. So for the 04, okay for 04, if ever na, I don't think Bell already told you, if you have any questions or clarifications and you need some clarification, I'm opening my Friday for you guys, so just inform me if you will be needing that time. If not na man, that would be very fine with me, that would be very fine with me kasi that is also outside my working hours na. So for today, we will be discussing about amino acid and proteins. The first few parts will actually be a review of your biochemistry. Okay, review of your biochemistry and may I just request some of you na you can unmute your mic if in case mawala ako bigla kasi hindi ko nakikita yung both Google Meet, I'm only on one Google Meet right now. Actually, I'm just on the power point, so please just inform me if things are not responding on your end. So for this morning, we will be discussing amino acids and protein, so hopefully I'll be able to finish. If you have seen my power point, that is the entire protein and that is a total of 77 slides. So for this morning, we will be discussing about amino acids, proteins and the different plasma protein. Right after amino acid and protein, we will be discussing liver function. We will be discussing liver function which is originally in clinical chemistry 2 nung tatlo pa ang clinical chem. But since the clinical chemistry now was cut short to only 2, it was cut short to only clinical chem 1 and clinical chem 2. Two of the topics from clinical chem 2 which are liver function and kidney function was carried out and transferred to clinical chemistry 1. So I'll just be discussing actually and I'm hoping that some of these terms are still familiar to you from your biochemistry. If not, I hope that you will listen intently and do extra reading in case that you don't understand or there are some topics that are still not clear to you. So let's start with amino acid. So for this morning, ay lang for this morning napu ako. So for today, we will be talking about the basic structure of your amino acid, the importance of its metabolism, some of the essential and non-essential and the new amino acids that has been discovered. We will also be going through amino acidopathies although the amino acidopathies I guess was already been discussed to you in your AUBF. So yung metabolic error, yung newborn metabolic, yung mga disorders like MSUD, alcaptanuria, tyrosiluria and others. And then we'll just have a quick one slide about amino acid analysis. So I hope all of you would now take out your power points and hopefully some of you now have printed the power point para makasunod kayo. So let's start. So first and foremost, in clinical chemistry, if you have realized by now, in clinical chemistry, there are three biomolecules that are mainly being discussed. Same thing in biochemistry, kung tutuosin nga, okay kung tutuosin, clinical chemistry is a re-echoed biochemistry. Because you did talk about carbohydrates na, you did talk about lipids na before and fats. You did talk about amino acid and proteins. You will also did talk about na hopefully before yung mga non-protein nitrogenous compounds like creatinine, yung uric acid among others. And even in zymology, which will be your first topic in clinical chemistry to next semester. So all of those things are already been discussed. But maybe some of you are wondering, sir, why is it that we're repeating it then in clinical chemistry one? Because now we're actually interjecting the clinical aspect in the biochemistry. So let's start off with amino acid. So amino acids are the building blocks of protein. So meaning to say, all your polypeptide, all your proteins are first made up of amino acid. Later on, I'll be having a short discussion about the central dogma. So this amino acid, if you could remember, there are a lot of amino acids. There are a lot of amino acids. If you're looking at your clinical chemistry book right now, there are a lot of amino acids, both essential, non-essential, and the new one. So these amino acids are different from one another because of their chemical group. Because of the chemical group attached to them. And those chemical group attached to them, or the R group, as we call them in clinical chemistry, give out unique chemical properties in each of the amino acids. So each of the amino acids are unique because of their chemical properties. And because of those chemical properties, each of these amino acids now would have a different biologic activity when now combined as a polypeptide or as a protein. So some amino acids function for growth and repair and even in the maintenance of your cell. And then there are some amino acids that are used for the production of your acetylcoenzyme A. There are some amino acids that are used to be converted as glucose in your gluconeogenesis. So there are a lot of amino acids and they have specific function alongside with them. So these chemical properties again of your amino acid would determine the biologic activity of your protein. So take for example your insulin. Your insulin has your, if you've studied your pro insulin. So in my biochem that was my report. So noong ako ay second year. So in second year, my report was your insulin. And your insulin can function as it is because of the cystein. The cystein that has a sulfur or the disulfide bond. That enables your insulin now to produce or to perform its function. So kung makikita niyo doon, because of the different amino acid located or included in your protein. Nagiging unique yung performance or yung function ng ating mga proteins. So as for the basic structure of your amino acid, your amino acid contains at least one of both. One amino group in one carboxylic functional group. So here is your amino group and located in your alpha carbon is your carboxylic group. In your carboxylic group, this is where other amino acid would attach forming now your peptide bond. So yung isang amino acid mo dito dudodong sa carboxylic group. So yung amino group na yan at yung carboxylic group na ito will combine forming now your peptide bond. So please do remember that this R group here, this is the unique group for each of your amino acid na pinaguusapan natin kanina. So moving forward, now this is just a single amino acid. But the chain of amino acid collectively is called your polypeptide. And your polypeptide and a large polypeptide now constitutes a protein. So technically in the human serum, proteins are around 100 to 150 amino acids. So each of your polypeptide chain inside your serum, in your plasma are around 100 to 150 amino acids. So here hindi lang siya mga dye, hindi lang siya, it's not just similar to carbohydrates na dysaccharide, monosaccharide or polysaccharide. Most actually of your proteins inside your body are in a form of polypeptide. Rather, most of your amino acids are in the form of your polypeptide. So just reiterating to you guys that amino acids again differ from one another by their chemical composition on their R group or their side chains. So there are around 20 different amino acids used as a building protein which I will be showing in a short while. So some of these are the essential and non-essential. So as you can see, these are your amino acids. You have your glycine all throughout until your proline. So let's just proceed on. I will not be discussing the structure naman na anymore. But here are the essential amino acid from the diet and then the amino acid that your body can produce. So disclaimer, when I say the body can produce, not all of this are immediately produced in your body. Like your tyrosine, take for example, your tyrosine would come from the catabolism of your phenylalanine. So some of this amino acid that can be produced inside your body are just results of your amino acid catabolism. So we have here the essential amino acid from your diet and the amino acid that your body can produce. So obviously, the one on your left are those that are from the diet. Meaning to say you cannot produce that, your body cannot produce that. That is the reason why. Even if I don't know, I'm not so clear about the clear difference between a vegan and a vegetarian. The reason why most vegetarians still need a protein substitute, most of the protein kasi natin are your meat, your egg, your face, lahat ng meat natin, those are your protein sources. That's why they need to look for other protein or plant based or vegetable based protein sources because they cannot simply just eradicate protein on their diet. If you eradicate protein on your diet or eradicate amino acid from your diet, what would happen to your body? Automatically, your body would not have enough amino acid to produce your protein. And your DNA replication would now be disrupted. Ito yung makakasira ng DNA mo at hindi yung vaccine ng COVID-19. Hindi yung COVID-19. So please do remember that amino acids are very important. So question, the big question siguro on your mind right now. Sir, are you gonna let us memorize these 20 amino acids? No. I will not. Because I am not letting you memorize that because there is another thing that I would let you memorize and not this one. So these are the essential amino acids again coming from their diet and the amino acids that are coming that your body can produce. So ito na lang yung tatandaan yung dalawa because this is new. This is new. Your two new amino acids. There are two amino acids that are included and that are considered to be new. So we have your selenocysteine and your pyrolysin. Sir, why do you consider it or why do we call it now recently identified amino acid? Because originally, if you have read your book already, both your selenocysteine and your pyrolysin are amino acids that were coded from a stop codon. So remember naman your stop codon, from biochem, from cytogen because you will count the stop codon when it comes to mulbion XM. So do you clear back when I say stop codon? Your stop codon are trinoclutide, your codon that would signal the cessation or the stoppage of your protein translation. That's the ideal. Pag rating ng transfer RNA mo sa stop codon, stop na lahat ng translation. Ang nangyari may na-code na protein for UGA from your UGA and that is now your pyrolysin. That is now your selenocysteine rather. That is now your selenocysteine. So these amino acids are new so please take note of this too and familiarize yourself na lang din with this too. Most importantly, among all the amino acids that I've shown you. Before that, let's now go to your amino acidopathies. The amino acidopathies question. Are all of this discussed na already in your AUBF? Can I just see Mil De bago ko pa tanongin na itapapachat ko dapat nag thumbs up na siya? So I guess it was all discussed naman na to you guys. So before kasi, I had to discuss this in clinical chemistry one because AUBF is in the second semester. Second sem kasi ang AUBF. So some of this are your PKU, your tyrosinemia, alcaptonuria, MSUD, isovallaric acidemia, homocystinuria, citrolinemia, your arginosocinic aciduria, and your cystinuria. Some of this, we will be discussing na lang. I have seen some of you mention that there are some that was not discussed. So I will be including this when we discuss our abnormalities and diseases comes your liver function. So moving forward now, quick analang, amino acid analysis. So analysis of amino acid lang to pagusapan natin. Hanot the protein in general pa lang. So when collecting blood samples for your amino acid analysis, blood should be drawn at least six to eight hours from a six to eight hours fast thing. So the patient should have fasted for six to eight hours before amino acid will be collected. And maybe some of you will be wondering, sir, why do we need fasting pa po in measuring your amino acid? So please do remember that for you to be able to have a better perspective of how much of the proteins or amino acid there is in your body. You have to fast because again, there are some amino acid that are coming from your diet. Ganon lang lag yun, everyone. Ganon lang lag yun. If some of the analytes that you will be measuring in your diet, you need to fast. Like, for example, your triglyceride. Why do I need to fast for triglyceride? Because there are such things called your exogenous triglyceride coming from your dietary intake. So when I eat, there will be lipids. And when I immediately, kapag kirunan ako ng dogok, makapuha din yung exogenous triglyceride ko. Same principle when it comes to your amino acid. Same principle when your amino acid. So moving forward, that in itself now is your amino acid. That is already your amino acid. I will just try to partition all my lectures. So I am actually going to finish until proteins, which is my entire goal naman for today, which is to finish until proteins. So I cannot pause a recording. So I will just stop it, if ever. So may questions ba? Do you have any questions? Clarification from both Google Meet. Mag-grace talang kayang hands so that it will like make to know so I can go to that. Are there any questions here from O2? Okay, from the main plenary. Okay, from the main room. Okay, so hindi na naman po ako pinapansin nang mga. Tatlong section na po yung nandito, hindi po sila sumasa ko. Are there any questions? Okay, Nanda sabi ni Chua. Okay, si Chua pa na taga-outo din. Okay, so moving forward. Let's go now to the... Nagigets ko rin naman, if wala ang question, because that is just an entire review for you guys. So let's go to proteins now. So proteins, sabi nga natin kanina, proteins is already a polymer of your amino acid. Okay, so there are other way I can phrase your proteins. So proteins are polymer of your amino acids. So tabi nga natin, okay, your proteins are very one of the... for me, hi, if I would actually choose if there are top molecules inside my body, that would be those three. Carbohydrates, lipids, and protein. Carbohydrates, lipid, and protein. So those are really just amas na lagi dapat natin alam. Even when you go to med school, you will still be discussing about these things. So going to protein now, protein comes from the Greek word protease, which means first rank of importance. And now later on my next slide, you will now realize why protein are called by the Greek one of the most first rank of importance or why is it very important. So please do take note that proteins can be composed of one or more unbranched chain of amino acid, which will be discussed further when we go to their structure. So you have a primary, secondary, tertiary and your quaternary protein. So all those four proteins are important and are different from one another. So most of your plasma protein, I want you to listen to this, underline this. Almost all of your plasma proteins are synthesized in your liver, specifically in your hepatocytes. So all of your proteins, lahatang proteins na nang iisip mo ngayon are secreted from your hepatocytes. So they are all produced in your liver except for one. What is that one? What is that except? Except for your immunoglobulins. Which will be discussed further next semester in your immunology and serology. So your immunology and your serology. So again, your proteins, all of your proteins are secreted and produced and synthesized in your liver except for your immunoglobulin. Except for your immunoglobulins that are secreted from your plasma cell. And your plasma cell are what type of cell originally? What is the... Your plasma cell are what type of cells? B cell, okay. B cell is a type of what double UBC? B cell is A? Infosite, okay. Your B cell is a CD4 or CD8? Your B cell is a CD4 or CD8? Halawa lang sumasagot. The answer is non. Because your CD4 and CD8 are T cells and not B cells. So gising gising na tayo, okay. So your B cells are not CD4. They are not CD8. They are for your T cells. Those are for your T cells. So moving forward, okay. Let us talk about how proteins are synthesized. How proteins are synthesized. I don't know why you called it first rank of importance. It's because proteins are the very first molecule your DNA will be creating, okay. It is the first biomolecule that they will be creating. Sir, hindi po carbs? Sir, hindi po carbohydrates? Sir, hindi po fats and lipids? No, but rather your protein. So in the central dogma, this is now how your DNA becomes your RNA and eventually becomes your protein, which is now your cells, your proteins which are now your organs, your proteins which are now your plasma, your proteins which are now your hormones, your proteins which are now your enzymes. So in short, a lot of the things in your body right now are protein, okay. A lot of the things in your body right now are actually protein, okay. So yung mga nagpuprotein, yung mga naguwey protein na dyan di ba. So you would realize how important protein is in your muscle, in your muscle development. So protein are synthesized. So backtrack tayo, throwback tayo. Before protein becomes protein, it is actually just your double stranded DNA. So there are three distinct parts of your central dogma. What are those three? Can I see it from the chat box? What are those three? Okay, let me just call somebody from 04. So 04, welcome to the class. Okay, welcome to the class. So let's go with one of the 04 who's here right now. Parang hindi ko... Let's go with ano. Parang hindi... Complete ba ang 04 right now dito? Okay, 04, let's go to... Okay, let's go to Raro. Miss Raro, can you please unmute your mic? Are you there? Okay, so baka natatravel pa po yung message ko kay Miss Raro. Is she here? Anyone from 04? Who's awake na 04? Who can answer me? What are the three? Si na yun? Si Matt Nelson. Agong Matt. Ano yung... yung sa central dogma ba di ba? Replication, transcription and translation. Replication, transcription and translation. Can you elaborate the three for us? Alam. What is your application? Elaborate po. Replication yung... From the name itself po, yung co-replicate po na ano. Yung DNA po. Then yung translation po is yung pag-converter ko na ano. Yung DNA to RNA. Pwede rin po siyang mag-reverse. And they're gonna reverse the transcription because the reverse transcription is po. Pwede rin po, yung action na yung different kinds of RNA to produce a protein po. So what do you call that process na nakuproduce ng protein? Yung translation. Translation. What are those three? You said that there are different types of RNA. What are those different types of RNA? CmRNA, CtrNA, and RNA. RNA? RRNA. RRNA. Question. Matt did mention about reverse transcription. Question. Does it happen in the human body? Does reverse transcription happen in your body? Let's go to Davis. Davis, can... Thank you Matt. So let's go to Davis. Davis, can reverse transcription happen in the human body? Ay... Ano sir? No po. No, why? Um, nakakit nga pa. Wait nang sir. Sir, di ba po sa HIV sa virus lang po yun? Parang ganun. So it's not in your body. How did you think na sa virus lang? Um, sabi sa bakte sir eh. Sabi sa bakte. Okay. Okay. Nama naman sa... But let us go to gusto kumarinik yung mga over. Let us go to let us go to sabayo. Let us go to sabayo. Why is it that humans cannot do reverse transcription? Ren. Okay. So color friend, sinong tataw, sinong masuerte, mo ang kaibigan, ang sasagot ng katanungan. Type it in. Ren, who's gonna answer? Hannah Ray. Hannah, are you here? Why is it that your um, you cannot perform reverse transcription? Sir, guess lang po. Yes sir po, wala po ang enzyme yung humans po ng reverse transcription. So impossible po na, makaron ang reverse transcription in our body. Thank you so much Miss Hannah. That's the answer. So even if sabihin na natin proteins are enzymes are proteins, your body doesn't have genetic code to produce the enzyme that will now um, do your reverse transcription. So your reverse transcription tastes, just like your SARS-CoV right now. Your SARS-CoV can do that. Your HIV can do that. So a lot of your RNA viruses can actually do reverse transcription. Okay? They can do reverse transcription. So again, picking it up from what Matt said, the central dogma is composed of three um, important processes which are your replication, your transcription and your translation. In your translation, there are three RNA involve your messenger RNA which is the template now for, for protein translation. You have next is your, your transfer RNA in your ribosomal RNA, your RNA. So all of those three are very important when it comes to translation, okay? So so much about that. Hindi I will not be talking about the central dogma as dissected as it is na pag-usapan pa natin yung okazaki fragments, the lagging and the lagging and the forward strand not anymore because that will be part of the bio, the mole bio that you will be having next semester. So having said that now, okay, having said that now, that now that you know the very important processes in the production of your protein, your protein can actually appear in different forms. We have your primary, your secondary tertiary and your quaternary um, protein structure. So when I say protein structure, okay, this are different pa from the simple and the conjugated, okay? When we are talking about structure, we're talking about its chemical structure, okay? So we have we have four. We have your primary, secondary, tertiary and your quaternary. Your primary your primary proteins are just a linear sequence of your amino acid. As you can see here, okay, this is just a linear okay, linear um, form of amino acid and pag sinabi natin linear meaning to say there are no um, there are no curve, there are no um, disulfide bonds here. There are no electrostatic interactions that would make it um, non-linear as to like your secondary until your quaternary um, protein structure. So your primary are linear sequence of amino acids. That's what I want you to remember. Now comes your um, secondary protein structure. Your secondary protein structure can be here in your alpha or your beta helix. Your alpha helix or a beta-plated um, um, protein. So as you can see here you have your alpha helix and you have your beta-plated sheet, okay? You have your beta-plated sheet. So this are repeating structure with hydrogen bonds. So the hydrogen bonds now increases the strength and the flexibility of your protein, okay? But there are more stronger um, protein structure which are now in the form of your tertiary and your quaternary protein. Your tertiary, okay, sir, what is the difference among all of this? Okay, among all of this. Did you know that the differences in their structure are brought about by the different, different amino acid that are found in each of this, in each of this proteins, okay? In each of these proteins. So your tertiary, take for example you have here now hydrophobic effect, ionic attraction, hydrogen bonds, and disulfide bonds. And as you can see in the tertiary tinawag natin siyang interactions and attraction. Because these are actually interactions among different amino acid. So take for example your disulfide can be found in two amino acid containing your sulfur, okay? So that is either your sustain, okay? Or your methionine. In other cases, you can also see other bonds like your hydrogen bond, your hydrophobic bond and at the same time your ionic bond. So that is what makes the tertiary enter, the tertiary um, structure of your protein more complex and more sturdy compared to your, compared to your primary and secondary. Now let's go to your quaternary amino acid. Sir what is the difference between quaternary amino acid? Quaternary proteins, rather, your quaternary um, protein are actually structures that result from interaction of more than one protein molecule. An example of this is your hemoglobin. Nakalala sa hemoglobin. Your hemoglobin has four globin chains, correct? Remember meron siyang apat na globin chain. Two alpha, two beta, which will become now your hemoglobin A, okay? So those four, okay? The interaction among those four um, the interaction among those four um, proteins, okay? Those are actually example of tertiary protein. Yung globin natin doon are example of tertiary proteins. Together, when they interact, okay? When those four interact, that will now become your quaternary structure, okay? So as you can see here, you have your alpha chain, alpha chain. This is your beta chain, this is your beta chain. This example here on your lower right is actually a hemoglobin, okay? It has an alpha chain and a beta chain, which is now what type of hemoglobin your hemoglobin A, okay? Your hemoglobin A. So please do remember, okay? Please do remember that this protein now, this protein are protein na by itself. So these are tertiary protein already. To be exact, these are actually these are alpha helix. This one in this particular example. So these are secondary. So these are secondary proteins joined together, now becoming a quaternary structure of your protein. Am I clear? Can I see a thumbs up if I am clear? So doon sa four, we have primary secondary tertiary and quaternary, okay? So moving forward now, okay? Wala doon sa Google Meet ng O2. So moving forward, so let's talk about the different properties of your protein. So your proteins can be classified according to their chemical properties, according to their function and according to their composition, okay? So that is now being simple or conjugated, okay? So let's go now to the charge and the isoelectric point, okay? To the isoelectric point. So your proteins can actually give out a positive or a negative charge. That's why we call your proteins amphoteric, okay? Amphoteric. So what do we mean by amphoteric? It can be um it can be positively charged or negatively charged isa pero isa lang. That is what you mean by amphoteric. A molecule that can either be positive or negatively charged. Sir, what is what do we call the molecule kapag both positive and negative charge siya at the same time, okay? At the same time. Paano pag merong isang molecule, okay? We call it your zwitter yun, correct? We call it your zwitter yun, okay? So zwitter yun does have both, they both have positive and negative charge at the very same time, okay? But as we are taking today, your proteins are amphoteric, okay? You're the the pH or the charge of your protein depends highly on your PI, okay? Hindi po ako nagmumura, okay? Or your isoelectric point, okay? The isoelectric point is a point where your protein are not negative or not negative. Simply charge less, okay? So if protein how can be placed in pH okay? In an environment where pH is greater than the isoelectric point, the protein will become positively charged, okay? Kapag pH naman is less than the PI, your protein now will become positively charged, okay? Will become positively charged. If pH is less than your PI, it will now become negative, it will now become positively charged, okay? It will now become positively charged. So this is actually explained by your Henderson-Hasselbach Equation. Your Henderson-Hasselbach Equation gives us now the relationship between your weak acid and your conjugate base, okay? So if pH is greater than your PI, proteins are negatively charged. If pH is less than your PI, your proteins are now positively charged. So usually, okay, the the pH where your your proteins are still soluble is around 5.5 to 8.0, okay? 5.5 to 8.0. That is the pH range for your protein. So again, what is your PI? Your PI is isoelectric point, a point where the number of positively charged is equal to the number of negatively charged group in a protein, okay? So meaning to say, it actually cancels out the charge, okay? It cancels out the charge. So but in the case na, okay? In the case na ang mangyare is that you are more positively charged and negatively charged. That is now in the case of changes in their pH, okay? Changes in the pH in relation to your in relation to your isoelectric point will now make it different, okay? Will now make it different. So moving forward now, I only have 5 minutes, okay? I only have 5 minutes. So don't worry nang mong question lang ako sa inyo. So let's talk about the solubility. So charge in the surface of your protein, obviously would affect their solubility, okay? Would affect their solubility. The solubility of your proteins is around pH 3.35 to 7.35 to 7.45. So the surface of, surface with charge will now become hydrophilic protein, which are the soluble type of protein. Question. Why is it that it is 7.35 to 7.45? Why is it that the optimal pH where your proteins are soluble is 7.35 to 7.45? So the answer is here na sa chuck box. Okay, let me check sa other. Normal pH of the blood, correct? Because this is the normal pH of the blood, correct? Tama naman kayo doon. That is the normal pH of your blood. So marapat lang na sa ganun pagkakataon soluble yung soluble yung ating protein. So that's correct, okay? So last 3 minutes, okay? So now going to your proteins, okay? Going out to our proteins, your proteins are very much prone to denaturation, okay? Denaturation is the loss of protein structure. And the loss in protein structure will lead to the loss of their function and their chemical characteristic, okay? Their chemical characteristic. And there are some reasons or some cases whereby your protein will be denatured. That is through exposure to hydrolysis because of strong acid or base. It can also be due to enzymatic, okay? So example lang enzymatic natin is your pepsin and your trypsin, urea exposure or other chemicals, and UV light exposure. So that is the reason why, di ba? Puntan po yung UV, no? UV light is why radiation, okay? Yung mga harmful na radiation, ha? That's why harmful radiation or your non-ionizing radiation is harmful to us because it can actually cause denaturation of your proteins, okay? Denaturation of your proteins and eventually causing even mutation in your DNA, okay? So exposure to that exposure to that will denature the protein inside your body, okay? So please do remember because when we talk about na the different types of procedures we're actually going to do denaturation to precipitate the protein, okay? To precipitate the protein. So to end this discussion, let me end my discussion by discussing to you the nitrogen balance, okay? Discussing to you the nitrogen balance. So unlike your fats that are stored as adipose unlike your carbohydrates that are stored as what? What is the storage form of your carbohydrates? Storage form of carbohydrates? Glycogen. What is the storage form of your ion? The soluble one. Soluble storage of ion 04 red 01 02 04 ready na. Nag-review na tayo. Veritine. What is the insoluble storage of ion? Hemosiderin, okay? Correct. Hemosiderin. So all of those all of those are storage are storage forms. So all of those compounds have their storage form unlike your nitrogen, okay? We do have amino acid pool in the liver, but we don't have a nitrogen storage. So there are no storage of nitrogen. That's why there are there is a need for us to have our amino acids or have our nitrogen coming from your diet. So a total of 16% of there is a total of 16% nitrogen content from the diet. So these are in the form of protein. Yung protein na na iniintake natin 16% of those are actually nitrogen. So what is nitrogen balance all about ba? Nitrogen balance is a state where your anabolism and catabolism are equal. Sir ano po yung anabolism? The synthesis, the production or the building up of a particular compound. Compared to catabolism, catabolism nag-cut of molecules, the breakdown of molecules. That is your catabolism. So we have your anabolism and your catabolism. If both are in equal rate, ibig sabihin sakto lang, parehas lang yung anabolism, same level lang or same rate lang din yung catabolism. That is now your nitrogen balance. That is your nitrogen balance. But what is now your what about now your positive balance? Ito siya. So your negative nitrogen balance is a state where the destruction is greater than the build up. So catabolism is greater than anabolism. So these are due to excessive tissue destruction like wasting diseases, continual high fever and starvation. Wasting disease, automatically this is a disease guys. That is why natin are being shed off or being excreted out of the body. Continual high fever. Why high fever? Remember that heat can denature your protein. Hence, it can destroy your protein increasing the rate of catabolism. What about starvation? Sir, bakit nagpagutom lang ako, hindi nagkaraon na ng negative? Why? Why is starvation included? Mr ok, tingnan natin. Ms. Velasco, why is starvation included in the negative nitrogen balance? Sir, sorry. Pedang palit pa na question. Why is starvation a cause of negative nitrogen balance? Sir, kasi during catabolism to the body will have to take up extra energy for to break down po. Yeah, but how is starvation related to the negative? Negative ano? Negative how would you call this negative nitrogen balance? Sir, starvation po kasi. What happened during starvation? Yung una mong sinabi about the energy, that's one side. Another is yun nang yon ako. Ok, so Ms. Velasco mentioned about your body using up the amino acids as energy source. Tama yun kasi wala kang carbohydrate source or whatsoever. But another thing is that there are no enough there are no longer enough amino acid because you are starving yourself and remember a lot of your essential amino acids are actually coming from your diet. So dahil dun, hindi rin ka, hindi ka rin magkakaroon ng anabolesim. So in the nitrogen balance the breakdown is greater than the synthesis. Unlike your protein, unlike your positive protein aside your, yeah, it's actually the promotion of gluconeogenesis. So in addition to that the positive nitrogen balance on the other hand, the production of protein is greater than yakatabolesim. The production of protein is greater than the breakdown of protein. This happened in your growth, in your pregnancy and in your repair. In growth, in your pregnancy and in your repair growth and repair. So another way to say it guys, another way to say it is that in negative nitrogen balance not only is katabolesim higher but excretion of nitrogen is also greater. What do we mean by greater? Ibig sabihin, I am releasing much of my nitrogen. Sure how? In the form of the bloodways, yung mga urea which we will be talking about pag nakarating tayo sa kidney function. So in your nitrogen, negative nitrogen your nitrogen was disposed. In your positive nitrogen dahil na increase yung anabolesim your nitrogen were retained. Less yung nitrogen excretion natin because you need the nitrogen to build up more protein to build up more protein in amino acid. So that is negative and positive nitrogen balance. So next meeting, which will be tomorrow, so we will be doing our discussion about the different classification of protein, be it protein na as an enzyme hormone, a transport protein among others. Different type of protein according to their structure which is simple and conjugated. So I will be ending this discussion now. So thank you so much for listening. So we will be continuing our discussion on clinical chemistry tomorrow because later