This document discusses non-protein amino acids (NPAAs), which perform important biological functions despite not being found in proteins. It categorizes NPAAs as alpha or non-alpha amino acids and provides examples of each, describing their roles and metabolic pathways. Key NPAAs discussed include ornithine, citrulline, arginosuccinic acid, thyroxine, triiodothyronine, S-adenosylmethionine, homocysteine, DOPA, creatinine, beta-alanine, GABA, and aminolevulinic acid. The document also notes that incorporation of some NPAAs into proteins is possible and discusses their potential relationships to diseases like autoimm
This document summarizes the biosynthesis of amino acids from key metabolic precursors. It discusses 6 families of amino acid biosynthesis defined by their precursor: (1) α-ketoglutarate family (glutamate, glutamine, proline, arginine), (2) 3-phosphoglycerate family (serine, glycine, cysteine), (3) oxaloacetate family (aspartate, asparagine, methionine, threonine, lysine), (4) pyruvate family (alanine, valine, leucine, isoleucine), (5) phosphoenolpyruvate and erythrose 4-phosphate family (tryptoph
Amino acids are biologically important organic compounds composed of amine (-NH2) and carboxylic acid (-COOH) functional groups, along with a side-chain specific to each amino acid. The key elements of an amino acid are carbon, hydrogen, oxygen, and nitrogen, though other elements are found in the side-chains of certain amino acids. About 500 amino acids are known and can be classified in many ways. They can be classified according to the core structural functional groups' locations as alpha- (α-), beta- (β-), gamma- (γ-) or delta- (δ-) amino acids; other categories relate to polarity, pH level, and side-chain group type (aliphatic, acyclic, aromatic, containing hydroxyl or sulfur, etc.). In the form of proteins, amino acids comprise the second-largest component (water is the largest) of human muscles, cells and other tissues.Outside proteins, amino acids perform critical roles in processes such as neurotransmitter transport and biosynthesis.
The document discusses the determination of the primary structure of proteins. It begins by explaining that proteins are composed of amino acid residues linked by peptide bonds to form a polypeptide chain. The primary structure refers to the specific sequence of amino acids in this chain. Mass spectrometry and tandem mass spectrometry techniques are used to analyze protein fragments obtained through enzymatic or chemical cleavage to determine the amino acid sequence and thereby elucidate the primary structure.
This document summarizes non-protein amino acids (NPAAs) and their roles and analysis. It discusses various alpha and non-alpha NPAAs like ornithine, citrulline, arginosuccinic acid, thyroxine, triiodothyroxine, and others. It describes their roles in biological pathways and diseases. The document also discusses methods for determining NPAAs and D-amino acids like capillary electrochromatography using chiral monolithic columns with fluorescence detection for high sensitivity.
Proteins fold into complex 3D structures essential for their function. There are four levels of protein structure - primary, secondary, tertiary, and quaternary. Chaperone proteins help other proteins fold correctly to prevent aggregation. Misfolded proteins can result from changes in temperature, pH, or lack of chaperones and may lead to disease if not degraded. Normally, misfolded proteins are targeted for degradation by the ubiquitin proteasome pathway, but accumulation of misfolded proteins can cause conditions like Alzheimer's disease.
The document summarizes the biosynthesis and metabolism of purines. It describes that purines are heterocyclic compounds consisting of two rings and are widely found in nature. There are two pathways for purine nucleotide synthesis - de novo synthesis which builds nucleotides from simple precursors, and the salvage pathway which recovers bases from degraded DNA and RNA. The de novo synthesis involves multiple steps using compounds from amino acids, formate, glycine and bicarbonate. Disorders of purine metabolism can cause hyperuricemia and gout due to deposition of urate crystals in joints. Lesch-Nyhan syndrome is a rare genetic disorder characterized by excessive uric acid production and self-mutilating behavior.
This document summarizes the biosynthesis of various amino acids from different metabolic precursors. It discusses 6 main families of amino acid biosynthesis defined by their precursor: (1) α-ketoglutarate family including glutamate, glutamine, proline, and arginine; (2) 3-phosphoglycerate family including serine, glycine, and cysteine; (3) oxaloacetate family including aspartate, asparagine, methionine, threonine, and lysine; (4) pyruvate family including alanine, valine, leucine, and isoleucine; (5) phosphoenolpyruvate and erythrose 4-phosphate
Secondary Structure Of Protein (Repeating structure of protein)Amrutha Hari
This document discusses the structure of proteins at various levels. It describes the primary, secondary, tertiary, and quaternary structures. The secondary structures discussed in detail include the alpha helix, beta pleated sheet, random coil, collagen helix, and beta turn. The alpha helix and beta pleated sheet are stabilized by hydrogen bonding between amino acids. The collagen helix structure provides strength and is the main component of connective tissues. Genetic disorders like Ehlers-Danlos syndrome and osteogenesis imperfecta result from defects in collagen structures. Ramachandran plots are used to visualize allowed backbone dihedral angles in protein structures.
This document summarizes the biosynthesis of amino acids from key metabolic precursors. It discusses 6 families of amino acid biosynthesis defined by their precursor: (1) α-ketoglutarate family (glutamate, glutamine, proline, arginine), (2) 3-phosphoglycerate family (serine, glycine, cysteine), (3) oxaloacetate family (aspartate, asparagine, methionine, threonine, lysine), (4) pyruvate family (alanine, valine, leucine, isoleucine), (5) phosphoenolpyruvate and erythrose 4-phosphate family (tryptoph
Amino acids are biologically important organic compounds composed of amine (-NH2) and carboxylic acid (-COOH) functional groups, along with a side-chain specific to each amino acid. The key elements of an amino acid are carbon, hydrogen, oxygen, and nitrogen, though other elements are found in the side-chains of certain amino acids. About 500 amino acids are known and can be classified in many ways. They can be classified according to the core structural functional groups' locations as alpha- (α-), beta- (β-), gamma- (γ-) or delta- (δ-) amino acids; other categories relate to polarity, pH level, and side-chain group type (aliphatic, acyclic, aromatic, containing hydroxyl or sulfur, etc.). In the form of proteins, amino acids comprise the second-largest component (water is the largest) of human muscles, cells and other tissues.Outside proteins, amino acids perform critical roles in processes such as neurotransmitter transport and biosynthesis.
The document discusses the determination of the primary structure of proteins. It begins by explaining that proteins are composed of amino acid residues linked by peptide bonds to form a polypeptide chain. The primary structure refers to the specific sequence of amino acids in this chain. Mass spectrometry and tandem mass spectrometry techniques are used to analyze protein fragments obtained through enzymatic or chemical cleavage to determine the amino acid sequence and thereby elucidate the primary structure.
This document summarizes non-protein amino acids (NPAAs) and their roles and analysis. It discusses various alpha and non-alpha NPAAs like ornithine, citrulline, arginosuccinic acid, thyroxine, triiodothyroxine, and others. It describes their roles in biological pathways and diseases. The document also discusses methods for determining NPAAs and D-amino acids like capillary electrochromatography using chiral monolithic columns with fluorescence detection for high sensitivity.
Proteins fold into complex 3D structures essential for their function. There are four levels of protein structure - primary, secondary, tertiary, and quaternary. Chaperone proteins help other proteins fold correctly to prevent aggregation. Misfolded proteins can result from changes in temperature, pH, or lack of chaperones and may lead to disease if not degraded. Normally, misfolded proteins are targeted for degradation by the ubiquitin proteasome pathway, but accumulation of misfolded proteins can cause conditions like Alzheimer's disease.
The document summarizes the biosynthesis and metabolism of purines. It describes that purines are heterocyclic compounds consisting of two rings and are widely found in nature. There are two pathways for purine nucleotide synthesis - de novo synthesis which builds nucleotides from simple precursors, and the salvage pathway which recovers bases from degraded DNA and RNA. The de novo synthesis involves multiple steps using compounds from amino acids, formate, glycine and bicarbonate. Disorders of purine metabolism can cause hyperuricemia and gout due to deposition of urate crystals in joints. Lesch-Nyhan syndrome is a rare genetic disorder characterized by excessive uric acid production and self-mutilating behavior.
This document summarizes the biosynthesis of various amino acids from different metabolic precursors. It discusses 6 main families of amino acid biosynthesis defined by their precursor: (1) α-ketoglutarate family including glutamate, glutamine, proline, and arginine; (2) 3-phosphoglycerate family including serine, glycine, and cysteine; (3) oxaloacetate family including aspartate, asparagine, methionine, threonine, and lysine; (4) pyruvate family including alanine, valine, leucine, and isoleucine; (5) phosphoenolpyruvate and erythrose 4-phosphate
Secondary Structure Of Protein (Repeating structure of protein)Amrutha Hari
This document discusses the structure of proteins at various levels. It describes the primary, secondary, tertiary, and quaternary structures. The secondary structures discussed in detail include the alpha helix, beta pleated sheet, random coil, collagen helix, and beta turn. The alpha helix and beta pleated sheet are stabilized by hydrogen bonding between amino acids. The collagen helix structure provides strength and is the main component of connective tissues. Genetic disorders like Ehlers-Danlos syndrome and osteogenesis imperfecta result from defects in collagen structures. Ramachandran plots are used to visualize allowed backbone dihedral angles in protein structures.
post translational modifications of proteinAnandhan Ctry
Post-translational modifications (PTMs) are chemical modifications of proteins that occur after translation. PTMs play a key role in regulating protein function by modifying activity, localization, and interactions. The main types of PTMs discussed are phosphorylation, glycosylation, ubiquitination, S-nitrosylation, methylation, N-acetylation, lipidation, and proteolysis. These modifications are identified through techniques like mass spectrometry, HPLC, radioactive labeling, and gel electrophoresis. PTMs are important for processes like cell signaling, growth, and apoptosis.
Gives in detail primary, secondary, tertiary and Quaternary structure of proteins. Gives classification of secondary structure: alpha helix, beta pleated sheet and different types of tight turns and explains most commonly found tight turn in proteins i.e. beta turn. Briefs about the Ramachandran plot of proteins, dihedral or torsion angles and explains why glycine and proline act as alpha helix breakers. Explains tertiary structure of proteins and different covalent and non covalent bonds in the tertiary structure and relative importance of these bonding interactions. Details about the quaternary structure of proteins and explains why hemoglobin is a quaternary protein and insulin is not.
Pyruvate is converted to acetyl CoA by the pyruvate dehydrogenase (PDH) complex in the mitochondria. PDH is a multi-enzyme complex containing five coenzymes and three enzymes that catalyzes the oxidative decarboxylation of pyruvate. This generates acetyl CoA, NADH, and FADH2, with the NADH and FADH2 contributing to ATP production through oxidative phosphorylation. PDH activity is regulated by phosphorylation/dephosphorylation and end-product inhibition by acetyl CoA and NADH.
- Amino acids are the building blocks of proteins. The 20 common amino acids contain different functional groups like carboxylic acids, amines, and alcohols.
- At physiological pH, amino acids exist as zwitterions with both a positive and negative charge. They can behave as both acids and bases.
- The isoelectric point is the pH at which the amino acid has no net charge as it exists predominantly in its zwitterionic form. Titration curves can be used to determine the pKa values and isoelectric point of an amino acid.
The document discusses various topics related to protein structure and function. It defines different types of bonds in proteins including peptide bonds, disulfide bonds, and hydrogen bonds. It describes the 20 common amino acids that make up proteins and different secondary structures such as alpha helices and beta sheets. It discusses the four levels of protein structure - primary, secondary, tertiary, and quaternary structure. It also covers protein folding driven by hydrophobic interactions and hydrogen bonding, as well as denaturation of proteins.
1. Nucleotides consist of a nitrogenous base, sugar (ribose or deoxyribose), and phosphate. Purines and pyrimidines are synthesized via de novo or salvage pathways to form nucleotides.
2. Purine synthesis occurs in multiple steps starting from PRPP, with the purine ring built step-by-step. Pyrimidine synthesis involves first forming the pyrimidine ring and then attaching it to ribose-5-phosphate.
3. Errors in purine synthesis can cause diseases like gout, which results from excess uric acid in the blood due to defects in purine metabolism or uric acid excretion. Several drugs target purine synthesis
COVALENT MODIFICATION AND ZYMOGEN ACTIVATIONMariya Raju
1) Covalent modifications, both reversible and irreversible, play important roles in regulating enzyme function. Reversible modifications like phosphorylation fine-tune enzyme activity, while irreversible proteolysis activates zymogens into active enzymes.
2) Digestive enzymes like trypsinogen are synthesized as inactive zymogens to avoid unwanted catalysis, then activated through limited and specific proteolysis. This proteolysis removes inhibitory peptide sequences and allows catalytic activity.
3) Activation of zymogens through proteolytic cascades amplifies hormonal signals, allowing a small stimulus to elicit a large response. This cascade activation greatly increases the potency and efficiency of regulation compared to direct hormone binding.
1) Allosteric enzymes have additional sites called allosteric sites that are distinct from the active site. Binding of an effector molecule to these sites can induce a conformational change in the active site, increasing or decreasing the enzyme's activity.
2) There are two main models that describe allosteric regulation - the concerted model where binding causes simultaneous changes in all subunits, and the sequential model where changes occur sequentially.
3) Allosteric enzymes exhibit sigmoidal kinetics curves rather than traditional hyperbolic curves due to their cooperative binding behavior. Positive allosteric effectors increase enzyme activity while negative effectors decrease it.
Metabolism of essential and non essential amino acids 20mariagul6
This document summarizes the metabolism of essential and non-essential amino acids in humans. It explains that non-essential amino acids can be synthesized in the body, while essential amino acids cannot and must come from diet. It describes the two main pathways of amino acid metabolism as transamination and deamination. Transamination transfers amino groups between amino acids, while deamination removes amino groups to form ammonia. The carbon skeletons of amino acids can be broken down into seven key intermediates, determining if the amino acid is glucogenic, ketogenic, or both. Genetic defects in amino acid metabolism pathways can cause serious disease.
This document discusses the metabolism of amino acids. It begins by outlining common reactions like transamination and deamination that amino acids undergo to release ammonia. Transamination involves the transfer of amino groups between amino acids and keto acids, allowing for interconversion. Deamination results in the liberation of ammonia, which is used to synthesize urea via the urea cycle in the liver. The carbon skeletons of amino acids are converted to keto acids that can be used for energy production, glucose synthesis, or formation of fats/ketone bodies. The document then goes into more detail about specific processes involved in amino acid metabolism, including transamination, deamination, decarboxylation, the urea cycle,
This document discusses nucleotides, their synthesis and degradation. It covers the following key points:
1. Nucleotides are composed of a nucleoside (a nitrogenous base linked to a 5-carbon sugar) bound to one or more phosphate groups. They are the monomers that make up nucleic acids like RNA and DNA.
2. Purine nucleotides are synthesized de novo through a complex 10 step pathway beginning with phosphoribosyl pyrophosphate (PRPP) and ending with inosine monophosphate (IMP). Pyrimidine nucleotides can also be synthesized from PRPP.
3. Nucleotides can be broken down through both intracellular catabolism pathways that generate purine
The urea cycle is a metabolic pathway that occurs in the liver to convert excess nitrogen from amino acid catabolism into urea for excretion. It involves five enzymes and five steps to synthesize urea from ammonia and carbon dioxide. Defects in the urea cycle can cause hyperammonemia, where high ammonia levels impair the citric acid cycle and ATP production in the brain.
ATP synthase—also called FoF1 ATPase is the universal protein that terminates oxidative phosphorylation by synthesizing ATP from ADP and phosphate.
ATP Synthase is one of the most important enzymes found in the mitochondria of cells
Amino acids have several key properties:
1. They are amphoteric, taking on positive, negative, or neutral charges depending on pH. Their isoelectric point is when the net charge is neutral.
2. They have acidic and basic groups that allow them to undergo various chemical reactions like esterification, acylation, and reactions with carbonyl compounds.
3. When heated to high temperatures during cooking, amino acids can form mutagenic and potentially toxic compounds like acrylamide or heterocyclic amines. The Maillard reaction and Strecker degradation play important roles in these processes.
Nucleotide Biosynthesis involves 2 processes. one is Denovo synthesis and other is Salvage pathway. An outline of both the processes has given in this presentation.
The document provides an overview of nucleic acid metabolism and the synthesis of purines and pyrimidines. It discusses how nucleotides serve as building blocks for nucleic acids and how they are synthesized through both de novo and salvage pathways. The key steps in purine synthesis include the production of IMP from PRPP and glutamine, followed by conversion to AMP and GMP. Purines can also be salvaged from nucleic acid breakdown. Deoxyribonucleotides are synthesized from ribonucleotides by the enzyme ribonucleotide reductase. Defects in nucleotide synthesis can cause diseases.
Titration curve of amino acid by KK Sahu sirKAUSHAL SAHU
The document discusses the titration curves of amino acids. It begins by introducing amino acids, their structure, and classification. It then defines titration as a method to determine acid levels in a solution by adding a base. The document explains that amino acids can act as both acids and bases, existing in a zwitterionic form. It provides examples of titration curves for specific amino acids like lysine, aspartate, glutamate, and alanine. These curves allow estimation of ionizable group pKa values and understanding amino acid acid-base behavior.
The six-step de novo pyrimidine biosynthesis pathway converts aspartate and bicarbonate into UMP. The first step produces carbamoyl phosphate from glutamine and bicarbonate. Carbamoyl phosphate then reacts with aspartate to form carbamoyl aspartate. Ring closure produces dihydroorotate, which is oxidized to orotate. Orotate is attached to PRPP to form OMP. OMP is decarboxylated to produce the final product UMP. UMP can be further modified to CTP and other pyrimidine nucleotides. The pathway is regulated by feedback inhibition of early enzymes by end products.
Estimation of dna by diphenylamine methodjeevithaseyan
This document describes a method to estimate the concentration of DNA using diphenylamine. DNA reacts with diphenylamine under acidic conditions to form a blue-green complex. Various concentrations of a DNA standard are reacted with diphenylamine reagent and measured at 595nm to generate a standard curve. An unknown DNA sample is then reacted, measured and its concentration determined using the standard curve. Reagents, equipment, procedure and calculations are outlined to perform the diphenylamine method of DNA concentration estimation.
The document provides an overview of nitrogen metabolism. It discusses (1) the importance of nitrogen in proteins and nucleic acids, (2) the key anabolic processes of nitrogen fixation, amino acid synthesis and protein synthesis, and (3) the main catabolic processes of proteolysis, nitrification and denitrification. Nitrogen is obtained from the atmosphere through nitrogen fixation by bacteria and is used to synthesize amino acids and proteins essential for plant structure and function.
Conversion of amino acids into specialised productsapeksha40
The document discusses the conversion of various amino acids into specialized products and metabolic pathways. It notes that amino acids serve as precursors for many nitrogenous compounds like porphyrins, neurotransmitters, hormones, creatine, purines and pyrimidines. It then elaborates on the specialized products and metabolic roles of individual amino acids such as alanine, arginine, cysteine, glycine, histidine, methionine, serine, tryptophan and tyrosine. Non-α amino acids like β-alanine, β-aminobutyrate and γ-aminobutyrate are also discussed. Key pathways and products mentioned include glutathione, creatine, catecholamines,
Dr. manoj Conversion of Amino Acids into Specialised Products.pptxDrManojAcharya1
Amino acids serve as precursors to many specialized compounds in the body. They can be converted to porphyrins, neurotransmitters, hormones, creatine, purines, pyrimidines, and other nitrogenous compounds. For example, alanine transports ammonia and pyruvate between tissues. Arginine contributes to urea synthesis and the creatine pathway. Cysteine forms taurine and glutathione. Glycine forms bile acids, heme, glutathione, purines, and contributes to creatine. Methionine forms S-adenosyl methionine and contributes to polyamine synthesis. Serine contributes to sphingosine and purine/pyrimidine synthesis. T
post translational modifications of proteinAnandhan Ctry
Post-translational modifications (PTMs) are chemical modifications of proteins that occur after translation. PTMs play a key role in regulating protein function by modifying activity, localization, and interactions. The main types of PTMs discussed are phosphorylation, glycosylation, ubiquitination, S-nitrosylation, methylation, N-acetylation, lipidation, and proteolysis. These modifications are identified through techniques like mass spectrometry, HPLC, radioactive labeling, and gel electrophoresis. PTMs are important for processes like cell signaling, growth, and apoptosis.
Gives in detail primary, secondary, tertiary and Quaternary structure of proteins. Gives classification of secondary structure: alpha helix, beta pleated sheet and different types of tight turns and explains most commonly found tight turn in proteins i.e. beta turn. Briefs about the Ramachandran plot of proteins, dihedral or torsion angles and explains why glycine and proline act as alpha helix breakers. Explains tertiary structure of proteins and different covalent and non covalent bonds in the tertiary structure and relative importance of these bonding interactions. Details about the quaternary structure of proteins and explains why hemoglobin is a quaternary protein and insulin is not.
Pyruvate is converted to acetyl CoA by the pyruvate dehydrogenase (PDH) complex in the mitochondria. PDH is a multi-enzyme complex containing five coenzymes and three enzymes that catalyzes the oxidative decarboxylation of pyruvate. This generates acetyl CoA, NADH, and FADH2, with the NADH and FADH2 contributing to ATP production through oxidative phosphorylation. PDH activity is regulated by phosphorylation/dephosphorylation and end-product inhibition by acetyl CoA and NADH.
- Amino acids are the building blocks of proteins. The 20 common amino acids contain different functional groups like carboxylic acids, amines, and alcohols.
- At physiological pH, amino acids exist as zwitterions with both a positive and negative charge. They can behave as both acids and bases.
- The isoelectric point is the pH at which the amino acid has no net charge as it exists predominantly in its zwitterionic form. Titration curves can be used to determine the pKa values and isoelectric point of an amino acid.
The document discusses various topics related to protein structure and function. It defines different types of bonds in proteins including peptide bonds, disulfide bonds, and hydrogen bonds. It describes the 20 common amino acids that make up proteins and different secondary structures such as alpha helices and beta sheets. It discusses the four levels of protein structure - primary, secondary, tertiary, and quaternary structure. It also covers protein folding driven by hydrophobic interactions and hydrogen bonding, as well as denaturation of proteins.
1. Nucleotides consist of a nitrogenous base, sugar (ribose or deoxyribose), and phosphate. Purines and pyrimidines are synthesized via de novo or salvage pathways to form nucleotides.
2. Purine synthesis occurs in multiple steps starting from PRPP, with the purine ring built step-by-step. Pyrimidine synthesis involves first forming the pyrimidine ring and then attaching it to ribose-5-phosphate.
3. Errors in purine synthesis can cause diseases like gout, which results from excess uric acid in the blood due to defects in purine metabolism or uric acid excretion. Several drugs target purine synthesis
COVALENT MODIFICATION AND ZYMOGEN ACTIVATIONMariya Raju
1) Covalent modifications, both reversible and irreversible, play important roles in regulating enzyme function. Reversible modifications like phosphorylation fine-tune enzyme activity, while irreversible proteolysis activates zymogens into active enzymes.
2) Digestive enzymes like trypsinogen are synthesized as inactive zymogens to avoid unwanted catalysis, then activated through limited and specific proteolysis. This proteolysis removes inhibitory peptide sequences and allows catalytic activity.
3) Activation of zymogens through proteolytic cascades amplifies hormonal signals, allowing a small stimulus to elicit a large response. This cascade activation greatly increases the potency and efficiency of regulation compared to direct hormone binding.
1) Allosteric enzymes have additional sites called allosteric sites that are distinct from the active site. Binding of an effector molecule to these sites can induce a conformational change in the active site, increasing or decreasing the enzyme's activity.
2) There are two main models that describe allosteric regulation - the concerted model where binding causes simultaneous changes in all subunits, and the sequential model where changes occur sequentially.
3) Allosteric enzymes exhibit sigmoidal kinetics curves rather than traditional hyperbolic curves due to their cooperative binding behavior. Positive allosteric effectors increase enzyme activity while negative effectors decrease it.
Metabolism of essential and non essential amino acids 20mariagul6
This document summarizes the metabolism of essential and non-essential amino acids in humans. It explains that non-essential amino acids can be synthesized in the body, while essential amino acids cannot and must come from diet. It describes the two main pathways of amino acid metabolism as transamination and deamination. Transamination transfers amino groups between amino acids, while deamination removes amino groups to form ammonia. The carbon skeletons of amino acids can be broken down into seven key intermediates, determining if the amino acid is glucogenic, ketogenic, or both. Genetic defects in amino acid metabolism pathways can cause serious disease.
This document discusses the metabolism of amino acids. It begins by outlining common reactions like transamination and deamination that amino acids undergo to release ammonia. Transamination involves the transfer of amino groups between amino acids and keto acids, allowing for interconversion. Deamination results in the liberation of ammonia, which is used to synthesize urea via the urea cycle in the liver. The carbon skeletons of amino acids are converted to keto acids that can be used for energy production, glucose synthesis, or formation of fats/ketone bodies. The document then goes into more detail about specific processes involved in amino acid metabolism, including transamination, deamination, decarboxylation, the urea cycle,
This document discusses nucleotides, their synthesis and degradation. It covers the following key points:
1. Nucleotides are composed of a nucleoside (a nitrogenous base linked to a 5-carbon sugar) bound to one or more phosphate groups. They are the monomers that make up nucleic acids like RNA and DNA.
2. Purine nucleotides are synthesized de novo through a complex 10 step pathway beginning with phosphoribosyl pyrophosphate (PRPP) and ending with inosine monophosphate (IMP). Pyrimidine nucleotides can also be synthesized from PRPP.
3. Nucleotides can be broken down through both intracellular catabolism pathways that generate purine
The urea cycle is a metabolic pathway that occurs in the liver to convert excess nitrogen from amino acid catabolism into urea for excretion. It involves five enzymes and five steps to synthesize urea from ammonia and carbon dioxide. Defects in the urea cycle can cause hyperammonemia, where high ammonia levels impair the citric acid cycle and ATP production in the brain.
ATP synthase—also called FoF1 ATPase is the universal protein that terminates oxidative phosphorylation by synthesizing ATP from ADP and phosphate.
ATP Synthase is one of the most important enzymes found in the mitochondria of cells
Amino acids have several key properties:
1. They are amphoteric, taking on positive, negative, or neutral charges depending on pH. Their isoelectric point is when the net charge is neutral.
2. They have acidic and basic groups that allow them to undergo various chemical reactions like esterification, acylation, and reactions with carbonyl compounds.
3. When heated to high temperatures during cooking, amino acids can form mutagenic and potentially toxic compounds like acrylamide or heterocyclic amines. The Maillard reaction and Strecker degradation play important roles in these processes.
Nucleotide Biosynthesis involves 2 processes. one is Denovo synthesis and other is Salvage pathway. An outline of both the processes has given in this presentation.
The document provides an overview of nucleic acid metabolism and the synthesis of purines and pyrimidines. It discusses how nucleotides serve as building blocks for nucleic acids and how they are synthesized through both de novo and salvage pathways. The key steps in purine synthesis include the production of IMP from PRPP and glutamine, followed by conversion to AMP and GMP. Purines can also be salvaged from nucleic acid breakdown. Deoxyribonucleotides are synthesized from ribonucleotides by the enzyme ribonucleotide reductase. Defects in nucleotide synthesis can cause diseases.
Titration curve of amino acid by KK Sahu sirKAUSHAL SAHU
The document discusses the titration curves of amino acids. It begins by introducing amino acids, their structure, and classification. It then defines titration as a method to determine acid levels in a solution by adding a base. The document explains that amino acids can act as both acids and bases, existing in a zwitterionic form. It provides examples of titration curves for specific amino acids like lysine, aspartate, glutamate, and alanine. These curves allow estimation of ionizable group pKa values and understanding amino acid acid-base behavior.
The six-step de novo pyrimidine biosynthesis pathway converts aspartate and bicarbonate into UMP. The first step produces carbamoyl phosphate from glutamine and bicarbonate. Carbamoyl phosphate then reacts with aspartate to form carbamoyl aspartate. Ring closure produces dihydroorotate, which is oxidized to orotate. Orotate is attached to PRPP to form OMP. OMP is decarboxylated to produce the final product UMP. UMP can be further modified to CTP and other pyrimidine nucleotides. The pathway is regulated by feedback inhibition of early enzymes by end products.
Estimation of dna by diphenylamine methodjeevithaseyan
This document describes a method to estimate the concentration of DNA using diphenylamine. DNA reacts with diphenylamine under acidic conditions to form a blue-green complex. Various concentrations of a DNA standard are reacted with diphenylamine reagent and measured at 595nm to generate a standard curve. An unknown DNA sample is then reacted, measured and its concentration determined using the standard curve. Reagents, equipment, procedure and calculations are outlined to perform the diphenylamine method of DNA concentration estimation.
The document provides an overview of nitrogen metabolism. It discusses (1) the importance of nitrogen in proteins and nucleic acids, (2) the key anabolic processes of nitrogen fixation, amino acid synthesis and protein synthesis, and (3) the main catabolic processes of proteolysis, nitrification and denitrification. Nitrogen is obtained from the atmosphere through nitrogen fixation by bacteria and is used to synthesize amino acids and proteins essential for plant structure and function.
Conversion of amino acids into specialised productsapeksha40
The document discusses the conversion of various amino acids into specialized products and metabolic pathways. It notes that amino acids serve as precursors for many nitrogenous compounds like porphyrins, neurotransmitters, hormones, creatine, purines and pyrimidines. It then elaborates on the specialized products and metabolic roles of individual amino acids such as alanine, arginine, cysteine, glycine, histidine, methionine, serine, tryptophan and tyrosine. Non-α amino acids like β-alanine, β-aminobutyrate and γ-aminobutyrate are also discussed. Key pathways and products mentioned include glutathione, creatine, catecholamines,
Dr. manoj Conversion of Amino Acids into Specialised Products.pptxDrManojAcharya1
Amino acids serve as precursors to many specialized compounds in the body. They can be converted to porphyrins, neurotransmitters, hormones, creatine, purines, pyrimidines, and other nitrogenous compounds. For example, alanine transports ammonia and pyruvate between tissues. Arginine contributes to urea synthesis and the creatine pathway. Cysteine forms taurine and glutathione. Glycine forms bile acids, heme, glutathione, purines, and contributes to creatine. Methionine forms S-adenosyl methionine and contributes to polyamine synthesis. Serine contributes to sphingosine and purine/pyrimidine synthesis. T
This document summarizes amino acid metabolism and related metabolic disorders. It discusses the general reactions of amino acid metabolism including transamination, deamination, and decarboxylation. It also describes the urea cycle, disorders of the urea cycle, and catabolism of phenylalanine, tyrosine, and their related metabolic disorders like phenylketonuria and albinism. Additionally, it discusses the catabolism of heme, hyperbilirubinemia, and the synthesis and roles of serotonin, melatonin, dopamine, norepinephrine, and adrenaline.
This document discusses the metabolism of several amino acids that are precursors for important biological compounds. It focuses on the metabolism of tyrosine, tryptophan, and glutamate. Tyrosine is a precursor for catecholamines like dopamine and norepinephrine. It is also used to synthesize melanin, thyroxine, and triiodothyronine hormones. Tryptophan metabolism produces serotonin, melatonin, and niacin. Glutamate is converted to the inhibitory neurotransmitter GABA via the GABA shunt pathway in neurons. The document provides detailed enzymatic reaction steps and pathways for the biosynthesis and catabolism of these amino acid derivatives.
Tryptophan is an essential amino acid that is metabolized through two main pathways - the kynurenine pathway and serotonin pathway. The kynurenine pathway leads to the production of NAD+ and takes place mainly in the liver. This pathway involves the enzymes tryptophan pyrrolase and kynureninase. Deficiencies in these enzymes or vitamin B6 can cause reduced NAD+ synthesis and manifestations of pellagra. The serotonin pathway produces the neurotransmitter serotonin from tryptophan in various tissues like the brain, gut and blood platelets. Serotonin is involved in behaviors, sleep, and gastrointestinal function. Melatonin is also derived from serotonin metabolism and regulates circadian rhyth
Phenylalanine and tyrosine are aromatic amino acids that are important precursors for the synthesis of various biological compounds like melanin, thyroid hormones, and catecholamines. Phenylalanine is converted to tyrosine by the enzyme phenylalanine hydroxylase. The catabolism of phenylalanine and tyrosine involves transamination, oxidative decarboxylation, and ring cleavage reactions. Defects in these pathways can lead to disorders like phenylketonuria, albinism, alkaptonuria, and tyrosinemia. Tyrosine is also a precursor for melanin synthesis, thyroid hormone biosynthesis, and the biosynthesis of catecholamines like dopamine, norepinephrine, and epine
This document discusses nucleoproteins, which are genetic proteins that are also known as nucleoproteins. Nucleoproteins are largely composed of chromatin, which contains both protein and nucleic acid components. The protein components are histones or protamines, while the nucleic acid components are DNA and RNA. Nucleoproteins are involved in cell division and transmission of hereditary factors. The document then describes the specific protein and nucleic acid components in more detail.
The document summarizes various topics related to amino acid and protein metabolism. It discusses the metabolism of amino acids including transamination, deamination, and the urea cycle. It also covers the catabolism of phenylalanine, tyrosine, and associated metabolic disorders like phenylketonuria. Other topics covered include the synthesis and significance of serotonin, melatonin, catecholamines, and the catabolism of heme.
The document summarizes various topics related to amino acid and protein metabolism. It discusses the metabolism of amino acids including transamination, deamination, and the urea cycle. It also covers the catabolism of phenylalanine, tyrosine, and associated metabolic disorders like phenylketonuria. Other topics covered include the synthesis and significance of serotonin, melatonin, catecholamines, and the catabolism of heme.
Tryptophan can be metabolized through several pathways in the body. The major pathway involves the production of niacin, with about 97% of tryptophan molecules metabolized this way. A minor pathway produces serotonin and melatonin. Tryptophan is also a precursor for the neurotransmitter serotonin, which regulates mood, sleep, and other functions. Excess serotonin can lead to carcinoid tumors. Melatonin is derived from serotonin and regulates circadian rhythms. The main excretory products of tryptophan metabolism are indole compounds. Diseases like Hartnup's involve defects in tryptophan absorption and reabsorption.
This document discusses nitrogen metabolism, including nitrogen fixation, amino acid anabolism and catabolism, and purine catabolism. Nitrogen fixation incorporates nitrogen from the atmosphere into organic compounds through processes like symbiotic nitrogen fixation by microorganisms in plants. The urea cycle removes nitrogen from the body in the form of urea. Purine catabolism produces uric acid as its end product in humans and other primates, which can accumulate and cause gout.
Protein metabolism is more appropriately learnt as metabolism of Amino acid. The proteins on degradation(proteolysis) release individual amino acids. The amount of free amino acids distributed throught the body is called Amino acid pool. The amino acids undergo certain common reactions like transamination followed by deamination for the liberation of ammonia. The amino group of amino acids utilized for the formation of urea, which is the end product of protein metabolism
The document discusses various topics related to biochemistry and drug metabolism. It provides information on:
- Drug metabolism occurs primarily in the liver through two phases - phase I involves reactions like oxidation and phase II involves conjugation reactions.
- Cytochrome P450 enzymes play an important role in phase I reactions like oxidation, reduction and hydroxylation.
- The liver contains endoplasmic reticulum where many metabolic reactions take place, including breakdown of hemoglobin (HB).
- There are endogenous and exogenous substances, with endogenous substances produced naturally in the body.
This document discusses purine metabolism, including the biosynthesis and catabolism of purines. It covers several key points:
- Nucleotides are composed of a nitrogenous base, pentose sugar, and phosphate groups, and are building blocks for DNA and RNA. They also participate in energy production and carbohydrate metabolism.
- Purines are synthesized through de novo and salvage pathways. De novo synthesis builds the purine ring from simple precursors, while salvage pathways recover purines from nucleic acid breakdown.
- Adenine and guanine are formed through a series of reactions adding carbon and nitrogen atoms to ribose-5-phosphate. IMP is converted to AMP and GMP, which
The document provides an overview of topics in medical biochemistry including carbohydrate chemistry, lipid chemistry, proteins and amino acids, nucleic acids, enzymes, and lipid metabolism. Key points include the structures and properties of monosaccharides, disaccharides, and polysaccharides. Lipid structures such as fatty acids, phospholipids, and cholesterol are described. The basics of protein structure, amino acid chemistry, and nucleic acid structure are summarized. Enzyme kinetics concepts and classes of enzymes are covered. Finally, an overview of lipid metabolism and beta-oxidation is presented.
The document summarizes the urea cycle, which consists of a series of chemical reactions that occur in the liver to convert ammonia into urea for excretion. There are five enzymes involved in the five-step cycle. First, carbamoyl phosphate synthase converts ammonia and carbon dioxide into carbamoyl phosphate in the mitochondria. Second, ornithine transcarbamoylase produces citrulline from carbamoyl phosphate and ornithine, also in the mitochondria. Third, citrulline and aspartate are condensed by argininosuccinate synthetase to form argininosuccinate. Fourth, argininosuccinate lyase cleaves argininosuccinate into fumarate and arg
brief overview of metabolism of all the essential & non essential amino acids along with their metabolic defects and special proteins synthesized from them
This document summarizes the structures, metabolism, and roles of phenylalanine and tyrosine. It discusses how phenylalanine is converted to tyrosine in the liver by the enzyme phenylalanine hydroxylase. Tyrosine can then be used to synthesize important compounds like thyroid hormones, melanin, and catecholamines. The document also outlines several disorders related to phenylalanine and tyrosine metabolism, including phenylketonuria, tyrosinemia, alkaptonuria, and albinism.
1) Amoebae are single-celled organisms that can change shape by extending and retracting pseudopods. They are found across eukaryotic life and include pathogens.
2) Well-known pathogenic amoebae that can infect humans include Naegleria fowleri which causes meningoencephalitis, Entamoeba histolytica which causes dysentery, and Acanthamoeba which can cause keratitis or granulomatous amoebic encephalitis.
3) Amoebae move using pseudopods, feed through phagocytosis or pinocytosis, and can form protective cysts. Their life cycles and pathogenesis depend
Typhoid fever is a bacterial infection caused by Salmonella Typhi that spreads through contaminated food or water. It has varied symptoms over 4 stages including sustained high fever, abdominal pain, and delirium. Diagnosis involves blood or stool cultures and the Widal test. Treatment is with antibiotics like fluoroquinolones or cephalosporins. Prevention relies on sanitation, hygiene, and typhoid vaccines. Multidrug resistance is a growing problem requiring alternative treatments.
Filariasis is caused by thread-like parasitic roundworms that are spread by mosquitoes and black flies. The worms live in the lymphatic system and other parts of the body, and the females release microfilariae that circulate in the bloodstream. Over time, this can lead to elephantiasis with thickening of the skin. Diagnosis involves examining blood slides for microfilariae at specific times of day. Treatment includes medications that kill the microfilariae like diethylcarbamazine, ivermectin, and doxycycline. Controlling mosquitoes is also important for preventing the spread of filarial parasites.
- Swine influenza, or swine flu, is caused by influenza viruses that normally infect pigs. It can sometimes be transmitted from pigs to humans.
- Symptoms in humans are similar to regular flu symptoms like fever, cough, and sore throat. It spreads when people with the virus cough or sneeze.
- Treatment involves antiviral drugs, which work best if started within two days of symptoms. Vaccines are also available to prevent swine flu.
The document provides information on Ebola virus, including:
1. Ebola virus is classified in the genus Ebolavirus and family Filoviridae. There are 5 species that cause disease in humans, with Zaire ebolavirus having the highest fatality rate of up to 90%.
2. Ebola virus disease symptoms start suddenly and include fever, muscle pain, and headaches. Later symptoms include vomiting, diarrhea, and internal/external bleeding.
3. The virus is transmitted through contact with infected body fluids and tissue. Bats are believed to be the natural reservoir of the virus. There is no approved vaccine or treatment, though supportive care can increase survival.
Free radicals are molecules with unpaired electrons that are highly reactive. They are generated through oxidative metabolism and reactions involving oxygen. Common free radicals include superoxide, hydroxyl radicals, and lipid peroxyl radicals. While free radicals can cause damage to tissues, the body has antioxidant defenses like superoxide dismutase, catalase, glutathione peroxidase, and vitamins C and E that help neutralize free radicals. Antioxidants protect cells from the harmful effects of free radical formation and oxidative stress.
Gene expression in eukaryotes involves transcription of DNA in the nucleus, followed by RNA processing and transport of mRNA to the cytoplasm for translation. Eukaryotic genes contain both coding exons and non-coding introns. During transcription, RNA polymerase II binds promoters and transcription factors to initiate transcription. The primary transcript undergoes splicing to remove introns and join exons, producing mature mRNA for translation into protein.
Gene expression in eukaryotes involves transcription of DNA in the nucleus, processing and export of mRNA, and translation of mRNA on ribosomes in the cytoplasm. Eukaryotic genes contain both coding exons and non-coding introns; the exons must be spliced together to form mRNA before translation. Three RNA polymerases transcribe different types of RNA in the nucleus, with RNA polymerase II responsible for mRNA and some small nuclear RNAs. Precise binding of transcription factors to promoter elements upstream of genes is required for transcription initiation by RNA polymerase II.
The document summarizes electron transport and oxidative phosphorylation. It describes how electrons from NADH and FADH2 are transported via carriers in the mitochondrial electron transport system to oxygen, with energy released used to synthesize ATP. Protons are pumped from the mitochondrial matrix to the intermembrane space, building a proton gradient that drives ATP synthesis by ATP synthase as protons flow back into the matrix. This chemiosmotic coupling allows efficient conversion of electron potential energy to chemical energy in the form of ATP.
The document discusses the enzyme-linked immunosorbent assay (ELISA), a biochemical technique used to detect antibodies, antigens, or other molecules in a liquid sample. ELISA uses antibodies and color changing enzymes to identify target molecules. It is a sensitive, quantitative, and widely used technique in medicine and research. There are different types of ELISA including competitive, sandwich, and indirect methods depending on the target molecule being detected.
Energy balance occurs when energy intake from food matches energy expenditure by the body. Energy expenditure consists of basal metabolic rate (BMR), the energy required for basic body functions, thermic effect of activity and food, and adaptive thermogenesis. BMR accounts for 50-75% of total energy expenditure and can be estimated using formulas factoring in weight, height, age, and gender. Tracking energy intake and expenditure helps determine if a person has a surplus, deficit, or balance of calories.
Ethyl glucuronide (EtG) is a biomarker for detecting alcohol consumption between 1 day and 1 week. It is formed by conjugating ethanol with glucuronic acid in the liver. EtG can be measured in urine, blood, and hair samples and remains detectable for up to 90 hours after heavy drinking. Studies have found EtG to be a sensitive and specific marker of recent alcohol intake that helps address the need for a biomarker in the timeframe not covered by other alcohol markers. Liquid chromatography-mass spectrometry is commonly used to precisely measure EtG levels in various samples.
This document discusses electrophoresis, which separates charged compounds using an electric field. It moves negatively charged proteins in serum towards the anode at pH 8.6. Applications include separating serum proteins, lipoproteins, hemoglobin variants, and isoenzymes. Zone electrophoresis is commonly used and involves applying samples to a support medium like paper, cellulose acetate, or polyacrylamide gel. After separation, proteins are visualized through staining and quantified using densitometry. Serum protein electrophoresis is used to analyze the albumin and globulin percentages. Abnormal patterns can indicate conditions like multiple myeloma or liver cirrhosis.
This document discusses the metabolism of unsaturated fatty acids and eicosanoids. It notes that animals have limited ability to desaturate fatty acids and require certain polyunsaturated fatty acids from plants. These essential fatty acids give rise to eicosanoic acids that produce eicosanoids like prostaglandins and leukotrienes. The metabolism of unsaturated fatty acids involves desaturase and elongase enzyme systems. Deficiencies in essential fatty acids can cause growth and reproductive issues in rats.
This document provides an overview of electrophoresis, including:
1. Electrophoresis uses the migration of charged solutes or particles in a liquid medium under the influence of an electric field. It is widely used to separate biological molecules like proteins.
2. Particles with different charge-to-mass ratios migrate at different rates depending on factors like their net charge, size, and the pH and strength of the buffer solution. Agarose gel and polyacrylamide gel electrophoresis are commonly used techniques.
3. The general procedure involves separating the particles in an electric field, staining to visualize the bands, then detecting and quantifying the separated fractions. Automated systems now allow high-throughput processing of
Cytokines are proteins that are involved in cell signaling and communication during immune responses and inflammation. They modulate processes like immune cell differentiation, activation of lymphocytes and phagocytes, and the development of adaptive immunity. Corticosteroids suppress immunity by blocking cytokine synthesis and release. Cytokines play roles in diseases like cancer, rheumatoid arthritis, and septic shock by regulating immune and inflammatory processes. They can be measured clinically to monitor certain conditions.
This document discusses cortisol measurement and its importance in diagnosing conditions like Cushing's syndrome and Addison's disease. It describes the physiology of cortisol secretion and regulation by CRH and ACTH in the HPA axis. Methods for measuring cortisol in serum, urine, and saliva are also outlined, including their advantages and disadvantages. Total serum cortisol, 24-hour urinary free cortisol, and salivary free cortisol are the main tests discussed for assessing cortisol levels.
Colorimetry is a common analytical technique used in clinical laboratories to estimate biochemical substances. It involves measuring the color intensity of a colored solution, which is proportional to the concentration of the colored substance. The solution is passed through a colorimeter, which measures the amount of light absorbed. Beer's law and Lambert's law describe how the absorption is related to concentration and path length. The colorimeter contains a light source, filter to select the wavelength, cuvette to hold the sample, and detector to convert light intensity to an electrical signal. Standards and blanks are used for calibration. Colorimetry is used to estimate many substances in blood, urine, and cerebrospinal fluid.
Chromatography is a technique used to separate and identify the components of a mixture. It works by allowing the molecules present in the mixture to distribute themselves between a stationary and a mobile medium. Molecules that spend most of their time in the mobile phase are carried along faster. Gas liquid chromatography uses an unreactive gas as the mobile phase flowing through a tube, with an involatile liquid held on particles of a solid support as the stationary phase. Thin layer chromatography uses a liquid as the mobile phase flowing past a thin layer of powder on a solid support, with substances less attracted to the solid or more soluble in the liquid moving faster up the plate.
Chromatography is a technique used to separate and identify components of mixtures using the principle of partition between two phases, a stationary phase and a mobile phase. There are several types including paper, thin layer, and gas-liquid chromatography. Gas-liquid chromatography involves passing a sample through a column containing a stationary liquid phase using an inert gas as the mobile phase, which separates the components into individual peaks that can be analyzed to identify substances.
8 Surprising Reasons To Meditate 40 Minutes A Day That Can Change Your Life.pptxHolistified Wellness
We’re talking about Vedic Meditation, a form of meditation that has been around for at least 5,000 years. Back then, the people who lived in the Indus Valley, now known as India and Pakistan, practised meditation as a fundamental part of daily life. This knowledge that has given us yoga and Ayurveda, was known as Veda, hence the name Vedic. And though there are some written records, the practice has been passed down verbally from generation to generation.
These lecture slides, by Dr Sidra Arshad, offer a quick overview of the physiological basis of a normal electrocardiogram.
Learning objectives:
1. Define an electrocardiogram (ECG) and electrocardiography
2. Describe how dipoles generated by the heart produce the waveforms of the ECG
3. Describe the components of a normal electrocardiogram of a typical bipolar lead (limb II)
4. Differentiate between intervals and segments
5. Enlist some common indications for obtaining an ECG
6. Describe the flow of current around the heart during the cardiac cycle
7. Discuss the placement and polarity of the leads of electrocardiograph
8. Describe the normal electrocardiograms recorded from the limb leads and explain the physiological basis of the different records that are obtained
9. Define mean electrical vector (axis) of the heart and give the normal range
10. Define the mean QRS vector
11. Describe the axes of leads (hexagonal reference system)
12. Comprehend the vectorial analysis of the normal ECG
13. Determine the mean electrical axis of the ventricular QRS and appreciate the mean axis deviation
14. Explain the concepts of current of injury, J point, and their significance
Study Resources:
1. Chapter 11, Guyton and Hall Textbook of Medical Physiology, 14th edition
2. Chapter 9, Human Physiology - From Cells to Systems, Lauralee Sherwood, 9th edition
3. Chapter 29, Ganong’s Review of Medical Physiology, 26th edition
4. Electrocardiogram, StatPearls - https://www.ncbi.nlm.nih.gov/books/NBK549803/
5. ECG in Medical Practice by ABM Abdullah, 4th edition
6. Chapter 3, Cardiology Explained, https://www.ncbi.nlm.nih.gov/books/NBK2214/
7. ECG Basics, http://www.nataliescasebook.com/tag/e-c-g-basics
Promoting Wellbeing - Applied Social Psychology - Psychology SuperNotesPsychoTech Services
A proprietary approach developed by bringing together the best of learning theories from Psychology, design principles from the world of visualization, and pedagogical methods from over a decade of training experience, that enables you to: Learn better, faster!
Osteoporosis - Definition , Evaluation and Management .pdfJim Jacob Roy
Osteoporosis is an increasing cause of morbidity among the elderly.
In this document , a brief outline of osteoporosis is given , including the risk factors of osteoporosis fractures , the indications for testing bone mineral density and the management of osteoporosis
TEST BANK For Basic and Clinical Pharmacology, 14th Edition by Bertram G. Kat...rightmanforbloodline
TEST BANK For Basic and Clinical Pharmacology, 14th Edition by Bertram G. Katzung, Verified Chapters 1 - 66, Complete Newest Version.
TEST BANK For Basic and Clinical Pharmacology, 14th Edition by Bertram G. Katzung, Verified Chapters 1 - 66, Complete Newest Version.
TEST BANK For Basic and Clinical Pharmacology, 14th Edition by Bertram G. Katzung, Verified Chapters 1 - 66, Complete Newest Version.
TEST BANK For Basic and Clinical Pharmacology, 14th Edition by Bertram G. Katzung, Verified Chapters 1 - 66, Complete Newest Version.
Local Advanced Lung Cancer: Artificial Intelligence, Synergetics, Complex Sys...Oleg Kshivets
Overall life span (LS) was 1671.7±1721.6 days and cumulative 5YS reached 62.4%, 10 years – 50.4%, 20 years – 44.6%. 94 LCP lived more than 5 years without cancer (LS=2958.6±1723.6 days), 22 – more than 10 years (LS=5571±1841.8 days). 67 LCP died because of LC (LS=471.9±344 days). AT significantly improved 5YS (68% vs. 53.7%) (P=0.028 by log-rank test). Cox modeling displayed that 5YS of LCP significantly depended on: N0-N12, T3-4, blood cell circuit, cell ratio factors (ratio between cancer cells-CC and blood cells subpopulations), LC cell dynamics, recalcification time, heparin tolerance, prothrombin index, protein, AT, procedure type (P=0.000-0.031). Neural networks, genetic algorithm selection and bootstrap simulation revealed relationships between 5YS and N0-12 (rank=1), thrombocytes/CC (rank=2), segmented neutrophils/CC (3), eosinophils/CC (4), erythrocytes/CC (5), healthy cells/CC (6), lymphocytes/CC (7), stick neutrophils/CC (8), leucocytes/CC (9), monocytes/CC (10). Correct prediction of 5YS was 100% by neural networks computing (error=0.000; area under ROC curve=1.0).
Does Over-Masturbation Contribute to Chronic Prostatitis.pptxwalterHu5
In some case, your chronic prostatitis may be related to over-masturbation. Generally, natural medicine Diuretic and Anti-inflammatory Pill can help mee get a cure.
2. Non protein amino acids
These amino acids, although never found
in proteins, perform several biological
important function.
These NPAAs and D-AA speculated to be
related to auto immune disease and to
aging
3. understand the role of NPAAs and D-
AA s in auto immune disease and
aging, the determination of these
NPAAs and D-AA s is required.
any nonprotein amino acid can be
chemically incorporated into peptides,
provided that appropriate methods are
designed for protecting the functional
group.
4. Nonprotein amino acids with no
cytotoxicity have been known to be
incorporated into proteins. For examples,
tyrosine and tryptophan residues in some
proteins have been substituted with m-
fluorotyrosine and 4-fluorotryptophan
respectively, without any effects on the
protein functions, and the 19F nuclei have
been used as magnetic resonance
5. One NPA that has received some attention is canavanine,
(L-2-amino-4-(guanidinooxy)butyric acid), the
guanidinooxy structural analogue of arginine.
These non protien amino acids are classified as alpha
and non alpha amino acids
1) Alpha amino acids:
a) ornithine
b) citruline
c) arginosuccinic acid
d) thyroxine
e) triodothyroxine
f) S-Adenosylmethionine
g) Homocysteine
h) 3,4-Dihydroxy phenylalanine ( DOPA)
I ) creatinine
j) ovathiol
k) Azaserine
6. 2) NON ALPHA amino acids:
a) beta –alanine
b) beta – aminoisobutyric acid
c) gama – aminobutyric acid(GABA)
d) aminolevulinic acid (ALA)
e) taurine
7. Alpha - aminoacids
1) ornithine :
ornithine is precursors of polyamine
Hydrolytic cleavage of the guanidino group of
arginine, catalyzed by liver arginase, releases urea .
The other product, ornithine, reenters liver
mitochondria and participates in additional rounds of
urea synthesis.
Ornithine and lysine are potent inhibitors of arginase,
and compete with arginine.
Arginine also serves as the precursor of the potent
muscle relaxant nitric oxide (NO) in a Ca2+-
dependent reaction catalyzed by NO synthase
2) Citrulline :
Citrulline is intermediates in the biosynthesis of urea
8.
L-Ornithine transcarbamoylase catalyzes
transfer of the carbamoyl group of carbamoyl
phosphate to ornithine,forming citrulline &
orthophosphate While the reaction occurs in
the mitochondrial matrix, both the formation of
ornithine and the subsequent metabolism of
citrulline take place in the cytosol.
Entry of ornithine into mitochondria and
exodus of citrulline from mitochondria
therefore involve mitochondrial inner
membrane transport systems
9. Arginosuccinic acid :
Arginosuccinic acid is intermediates in
the biosynthesis of urea
Argininosuccinate synthetase links
aspartate and citrulline via the amino group
of aspartate and provides the second
nitrogen of urea.
The reaction requires ATP and involves
intermediate formation of citrullyl-AMP.
Subsequent displacement of AMP by
aspartate then forms arginosuccinate.
10. In addition to patients that lack
detectable argininosuccinate
synthetase activity a 25-fold elevated
Km for citrulline has been reported. In
the resulting citrullinemia, plasma and
cerebrospinal fluid citrulline levels are
elevated, and 1–2 g of citrulline are
excreted daily.
11. 4) Thyrosine and triodothyroxine
:
Tyrosine forms norepinephrine and
epinephrine, and following iodination the
thyroid hormones triiodothyronine and
thyroxine.
Use of measurement of blood thyroxine
or thyroid-stimulating hormone (TSH) in
the neonatal diagnosis of congenital
hypothyroidism.
The amino acid tyrosine is the starting
point in the synthesis of the
catecholamines and of the thyroid
hormones tetraiodothyronine (thyroxine;
T4 ) and triiodothyronine (T3)
12. thioredoxin reductase, glutathione
peroxidase, and the deiodinase that converts
thyroxine to triiodothyronine.
The clinical history, physical examination,
and lab results were all consistent with
primary hypothyroidism. Accordingly, the
patient was started on a low dose of
thyroxine (T4 ).
It is important to begin therapy with a small
dose of T4, as larger doses can precipitate
serious cardiac events, due to the changes in
metabolism caused by administration of the
hormone.
Thyroxine (T4), free: 4.0 pmol/L (normal
10.3–21.9 pmol/L)
13. 5)S-Adenosylmethinine
homocysteine:S-Adenosylmethionine, the principal source of methyl groups
in metabolism, contributes its carbon skeleton to the
biosynthesis of the polyamines spermine and spermidine.
Homocystinuria
Homocystinuria Cystathionine -synthase Lens dislocation,
thrombotic vascular disease, mental retardation, osteoporosis
AR
Homocystinuria
5,10-Methylenetetrahydrofolate reductase
Mental retardation, gait and psychiatric abnormalities,
recurrent strokes ,Mental retardation, hypotonia, seizures,
megaloblastic anemia
14. Pathways, enzymes, and coenzymes involved
in the homocystinurias. Methionine transfers a
methyl group during its conversion to
homocysteine.
Defects in methyl transfer or in the subsequent
metabolism of homocysteine by the pyridoxal
phosphate (vitamin B6)-dependent cystathionine
b-synthase increase plasma methionine levels.
Homocysteine is transformed into methionine via
remethylation. This occurs through methionine
synthase, a reaction requiring methylcobalamin
and folic acid.
Deficiencies in these enzymes or lack of cofactors
is associated with decreased or normal methionine
levels. In an alternative pathway, homocysteine
can be remethylated by betaine:homocysteine
methyl transferase
15. Life-threatening vascular complications
(affecting coronary, renal, and cerebral
arteries) can occur during the first decade of
life and are the major cause of morbidity and
mortality.
Classic homocystinuria can be diagnosed
with analysis of plasma amino acids,
showing elevated methionine and presence
of free homocystine.
16. Total plasma homocysteine is also extremely
elevated (usually >100 M). Treatment consists
of a special diet restricted in protein and
methionine and supplemented with cystine.
In approximately half of patients, oral
pyridoxine (25–500 mg/d) produces a decrease
in plasma methionine and homocystine
concentration in body fluids.
Folate and vitamin B12 deficiency should be
prevented by adequate supplementation.
Betaine is also effective in reducing
homocystine levels.
17.
18. 6) 3-4
Dihydrophenylalanine(DOPA):
Neural cells convert tyrosine to epinephrine and
norepinephrine. While dopa is also an intermediate in
the formation of melanin, different enzymes hydroxylate
tyrosine in melanocytes.
Dopa decarboxylase, a pyridoxal phosphate-dependent
enzyme, forms dopamine. Subsequent hydroxylation by
dopamine -oxidase then forms norepinephrine.
In the adrenal medulla, phenylethanolamine-N-
methyltransferase utilizes S-adenosylmethionine to
methylate the primary amine of norepinephrine, forming
epinephrine .
Tyrosine is also a precursor of triiodothyronine and
thyroxine.
DOPA ... related to dopaminerelationship to Parkinson's
Disease
19. Dopamine, Norepinephrine, and Epinephrine
1. SYNTHESIS OF THE CATECHOLAMINE
NEUROTRANSMITTERS
These three neurotransmitters are synthesized in a
common pathway from the amino acid L-tyrosine.
The first and rate-limiting step in the synthesis of these
neurotransmitters from tyrosine is the hydroxylation of
the tyrosine ring by tyrosine hydroxylase, a
tetrahydrobiopterin(BH4)-requiring enzyme. The
product formed is dihydroxyphenylalanine or DOPA.
The phenyl ring with two adjacent OH groups is a
catechol, andhence dopamine, norepinephrine, and
epinephrine are called catecholamines.
20. The second step in catecholamine synthesis is the
decarboxylation of DOPA to form dopamine. This
reaction, like many decarboxylation reactions of
amino acids,equires pyridoxal phosphate.
Dopaminergic neurons (neurons using dopamine
as a neurotransmitter) stop the synthesis at this
point, because these neurons do not synthesize
the enzymes required for the subsequent steps.
Neurons that secrete norepinephrine synthesize it
from dopamine in a hydroxylation reaction
catalyzed by dopamine -hydroxylase (DBH). This
enzyme is present only within the storage vesicles
of these cell
Although the adrenal medulla is the major site of
epinephrine synthesis, it is also synthesized in a
few neurons that use epinephrine as a
21.
22. 7)Creatinine :
Creatinine is formed in muscle from creatine
phosphate by irreversible, nonenzymatic
dehydration and loss of phosphate.
Since the 24-h urinary excretion of creatinine is
proportionate to muscle mass, it provides a
measure of whether a complete 24-h urine
specimen has been collected.
Glycine, arginine, and methionine all participate
in creatine biosynthesis. Synthesis of creatine
is completed by methylation of guanidoacetate
by S-adenosylmethionine.
25. 8) Ovathiol:-
Sulfur containing amino acid found in fertilized
Eggs, and acts as an antioxidant
9) Azaserine: (antibiotic)
Purine deficiency states, while rare in humans,
generally reflect a deficiency of folic acid.
Compounds that inhibit formation of
tetrahydrofolates and therefore block purine
synthesis have been used in cancer
chemotherapy.
Inhibitory compounds and the reactions they inhibit
include azaserine, diazanorleucine, 6-
mercaptopurine , and mycophenolic acid .
26. II) Non--Amino Acids:
Non--amino acids present in tissues in a free form
include -alanine, -aminoisobutyrate, and -aminobutyrate
(GABA). -Alanine is also present in combined form in
coenzyme A and in the -alanyl dipeptides carnosine,
anserine and homocarnosine .
1) Beta-Alanine & -Aminoisobutyrate :
Alanine and -aminoisobutyrate are formed during
catabolism of the pyrimidines uracil and thymine,
respectively . Traces of -alanine also result from the
hydrolysis of -alanyl dipeptides by the enzyme
carnosinase. -Aminoisobutyrate also arises by
transamination of methylmalonate semialdehyde, a
catabolite of L-valine .
The initial reaction of -alanine catabolism is
transamination to malonate semialdehyde. Subsequent
transfer of coenzyme A from succinyl-CoA forms
malonyl-CoA semialdehyde, which is then oxidized to
malonyl-CoA and decarboxylated to the amphibolic
intermediate acetyl-CoA.
27. Analogous reactions characterize the catabolism
of -aminoisobutyrate. Transamination forms
methylmalonate semialdehyde, which is converted
to the amphibolic intermediate succinyl-CoA by
reactions 8V and 9V of.
Disorders of -alanine and -aminoisobutyrate
metabolism arise from defects in enzymes of the
pyrimidine catabolic pathway.
Principal among these are disorders that result
from a total or partial deficiency of
dihydropyrimidine dehydrogenase.
28. 2) beta-Alanyl Dipeptides :
The -alanyl dipeptides carnosine and anserine
(N -methylcarnosine) activate myosin ATPase,
chelate copper, and enhance copper uptake. -
Alanyl-imidazole buffers the pH of anaerobically
contracting skeletal muscle.
Biosynthesis of carnosine is catalyzed by
carnosine synthetase in a two-stage reaction tha
involves initial formation of an enzyme-bound
acyl-adenylate of -alanine and subsequent
transfer of the -alanyl moiety to L-histidine.
29. Hydrolysis of carnosine to -alanine and L -
histidine is catalyzed by carnosinase. The
heritable disorder carnosinase deficiency is
characterized by carnosinuria.
Homocarnosine, present in human brain at
higher levels than carnosine, is synthesized in
brain tissue by carnosine synthetase. Serum
carnosinase does not hydrolyze
homocarnosine. Homocarnosinosis, a rare
genetic disorder, is associated with progressive
spastic paraplegia and mental retardation.
30. 3) gama-Aminobutyrate
gama-Aminobutyrate (GABA) functions in brain
tissue as an inhibitory neurotransmitter by
altering transmembrane potential differences.
GABA is formed by decarboxylation of
glutamate by L -glutamate decarboxylase.
Transamination of -aminobutyrate forms
succinate semialdehyde, which can be reduced
to -hydroxybutyrate by L -lactate
dehydrogenase, or be oxidized to succinate
and thence via the citric acid cycle to CO2 and
31. A rare genetic disorder of GABA metabolism
involves a defective GABA aminotransferase,
an enzyme that participates in the catabolism of
GABA subsequent to its postsynaptic release in
brain tissue.
Defects in succinic semialdehyde
dehydrogenase are responsible for another rare
metabolic disorder of -aminobutyrate
catabolism characterized by 4-hydroxybutyric
aciduria.
32.
33. 4) amino levulinic acid (ALA) :
ALA is intermediate in the synthesis of
porphyrin (finally heme)
34. 5) Taurine :
Taurine (2-aminoethylsulphonic acid) is a non-
protein
aminoacid present in almost all animal tissues and
the most abundant free intracellular aminoacid in
human cells.
In humans, it is considered to be a “semi-essential
aminoacid” since it can be synthesized from
other sulfonic aminoacids such as methionine and
cysteine, in
the presence of vitamin B6,2,3 but endogenous
production is insufficient, so that it needs to be
provided through diet.
35.
36. Biological effects of taurine in the context of
diabetes
Biological EffectMechanismof Taurine
Antioxidant action By inhibiting ROS generation
at mitochondria Osmoregulation By
counteracting osmotic inbalance through
cellular membrane due
to hyperglycaemia
Antiinflammatory effects By interfering the
formation of inflammatory mediators Glucose
Homeostasis By interfering the insulin
signalling pathway acting upon UCP2 protein
37. Estimation of NPAAs :
1) The aim of our study was to analyze NPAAs
and D-AA s in biosamples by means of capillary
electrochromatogrphy (CEC) using a chiral
practicle- loded monolithiac column with
flurrosense detection for high sensitivity.
2) capillary electrophoresis
3) High perfromance liquid
chromatography(HPLC)
4) laser-induced flurosecne (LIF)
5) scanning electro microscopy (SEM)
39. Location of the regions of ordered secondary structures for b-residues in
f–q–y space. The a-helix and b-sheet are the classical structures for poly a-
amino
acids. b-residues occurring in the appropriate shaded region can be