DOCSLIB.ORG

Rapid Review of Amino Acid Metabolism Cell Biology > Protein Synthesis > Protein Synthesis

Total Page：16

File Type：pdf, Size：1020Kb

Download full-text PDF Read full-text
Rapid Review of Amino Acid Metabolism Cell Biology > Protein Synthesis > Protein Synthesis Rapid Review of Amino Acid Metabolism Cell Biology > Protein Synthesis > Protein Synthesis AMINO ACID POOL OVERVIEW Amino acid pool • Describes all free amino acids in the body • Amino acids: body's primary source of nitrogen AMINO ACID STRUCTURE • Central carbon bound to: -H, -COOH, -NH3, R-group • R-group: acidic (-), basic (+), branched, etc. AMINO ACID POOL: INPUTS AND OUTPUTS Input • Dietary proteins: absorbed as amino acids/peptides in small intestine – Pass through hepatic portal vein and immediately enter liver – Liver plays central role in fates of free amino acids • De novo amino acid synthesis: use C-skeletons & alpha-amino group of other amino acids to synthesize new ones • Protein turnover: breakdown of cellular proteins Output • Oxidation: excess amino acids degraded to alpha amino group & C-skeleton – Urea cycle: liver rids body of nitrogen waste – Energy production: C-skeletons enter glycolysis or citric acid cycle – Gluconeogenesis: occurs in liver – Storage: amino acids can't be stored --> C-skeletons stored as glycogen/fats • Synthesis of nitrogen-containing molecules – Amino acids – Neurotransmitters – Nucleotides (purines and pyrimidines) – Creatine, etc. • Protein turnover: synthesis of new proteins 1 / 5 Protein turnover Cyclic synthesis and breakdown of proteins in the body • Produces and consumes free amino acids • Protein synthesis: depletes pool of free amino acids • Protein breakdown: replenishes pool ESSENTIAL AMINO ACIDS Must be obtained from diet • "My Tall Vegan Friend Is Watering Kale Leaves" – M, T, V, F, I, W, K, L • Glucogenic: Methionine, threonine, valine • Glucogenic & ketogenic: Phenylalanine, isoleucine, tryptophan • Ketogenic: lysine & leucine Branched chain amino acids (BCAA) • Valine, leucine, isoleucine • Immediately shunt from liver to circulation • Liver lacks an aminotransferase that muscle, adipose, kidney & brain have Aminotransferases: family of enzymes involved in amino acid breakdown NONESSENTIAL AMINO ACIDS Synthesized endogenously (The rest of the amino acids) Glucogenic: alanine, asparagine, aspartate, cysteine, glutamate, glutamine, glycine, histidine, proline & serine • Glucogenic and ketogenic: tyrosine • Histidine is often considered essential because it is essential during the first 5 years of life but later becomes nonessential. Note that there are many ways to categorize essential/nonessential amino acids CLINICAL CORRELATION Conditionally essential amino acids • Cannot be synthesized under certain physiologic conditions • Infants • Immunosuppressed patients/postoperative infections: treat w/ arginine & glutamine supplements FULL TEXT 2 / 5 Here we will learn an overview of amino acid metabolism, the primary source of nitrogen in the body. We will specifically learn about the amino acid pool. THE AMINO ACID POOL  Definitions • The amino acid pool describes all the free amino acids in the body. • Amino acids are the body's primary source of nitrogen. These include intracellular free amino acids as well as those in circulation. The structure of an amino acid • Draw a central carbon bound to a hydrogen. • Show that it binds an amino group on one side and a carboxyl group on the other. • Indicate that its fourth bond is with an R-group, a functional side group. Recall that the functional group can be acidic, basic, branched, etc. • Acidic amino acids are negatively charged at physiologic pH, and that basic amino acids are positively charged. Now that we've reviewed some basic characteristics of amino acids, let's learn how the content of our amino acid pool fluctuates. Free amino acids derive from three sources: • Dietary proteins, which are absorbed as amino acids and peptides in the small intestine. • De novo amino acid synthesis; we use carbon skeletons and the alpha-amino group of other amino acids to synthesize new ones. • Protein turnover, the breakdown of cellular proteins. AMINO ACID CONSUMPTION Show that free amino acids are consumed in the following ways: • Oxidation Oxidation is the process in which excess amino acids are broken down into an alpha amino group and a carbon skeleton. The products of this reaction may enter the major following metabolic pathways: – The urea cycle: occurs in the liver and rids the body of nitrogen waste. – Energy production: amino acid carbon skeletons can enter glycolysis or the citric acid cycle. – Gluconeogenesis: occurs in the liver. – Storage: amino acids themselves cannot be stored; their carbon skeletons are converted to glycogen or fats if they aren't used immediately. Thus, oxidation can shunt excess amino acids into a number of different metabolic pathways. • Synthesis of nitrogen-containing molecules – Synthesis of nitrogen-containing molecules includes amino acids themselves (de novo amino acid synthesis), 3 / 5 neurotransmitters, nucleotides (purines and pyrimidines) and creatine, amongst others. • Protein turnover – Protein turnover both produces and consumes free amino acids. PROTEIN TURNOVER Here, we draw-out protein turnover, which is the cyclic synthesis and breakdown of proteins in the body is called "Protein Turnover." • Draw the amino acid pool and show that free amino acids can enter and leave it. • Indicate that: – Protein synthesis depletes the pool of free amino acids. – Protein breakdown in the body replenishes the pool. However, not all amino acids in the pool are the same. Amino acids that are present in excess can be used to synthesize and replenish the pool with amino acids that are scarce. THE AMINO ACIDS Let's learn the amino acids, now. • Create a chart with two columns labeled essential and nonessential amino acids. ESSENTIAL AMINO ACIDS  Essential amino acids must be obtained from the diet, while nonessential amino acids can be synthesized endogenously. • The essential amino acids include: – Methionine, threonine, valine, phenylalanine, isoleucine, tryptophan, lysine, leucine (M, T, V, F, I, W, K, L). We can remember them by the following mnemonic: My Tall Vegan Friend Is Watering Kale Leaves. Note that histidine is sometimes considered an essential amino acid. Glucogenic vs Ketogenic amino acids • Glucogenic amino acids: methionine, threonine and valine • Ketogenic amino acids: leucine and lysine. Glucogenic and Ketogenic amino acids: phenylalanine, isoleucine, tryptophan. They can shunt into either pathway.* How do these essential amino acids enter gluconeogenesis or ketogenesis? • Answer: they enter the liver, the primary site of metabolic integration! Amino acid entrance into the liver. • Draw a segment of the small intestine and indicate that dietary amino acids (both essential and nonessential) are absorbed, here. • Show that they pass through the hepatic portal vein and enter the liver. 4 / 5 • Indicate that they may enter any of the three destinations that we illustrated in our amino acid pool diagram. • Branched-chain amino acids (BCAA) [valine, leucine and isoleucine] immediately leave the liver and enter the circulation. Branched-Chain Amino Acid (BCAA) Deamination The liver cannot deaminate branched-chain amino acids – deamination is the first step in amino acid breakdown. • Branched-chain amino acids travel to the muscle, which has a specific enzyme that can deaminate them. Branched-Chain Amino Acid Functional Roles Branched-chain amino acids play a number of important roles: • They provide hydrophobic side chains in protein structure. • They are used as a transport mechanism for nitrogen from the liver to the peripheral tissues. Muscle tissues can use these amino acids to synthesize nonessential amino acids. NONESSENTIAL AMINO ACIDS They include the "rest" of the amino acids. • alanine, arginine, asparagine, aspartate, cysteine, glutamate, glutamine, glycine, histidine, proline, serine and tyrosine. • All of them except for tyrosine are all glucogenic amino acids. Knowing their molecular make-up, we might expect this from amino acids that can be readily synthesized from carbon- skeletons in the body. • Tyrosine is a ketogenic amino acid. As a clinical correlation write that some amino acids are considered conditionally essential amino acids because they cannot be synthesized under certain physiologic or pathophysiologic conditions. • Infants and children up to 5 years old cannot synthesize: – Arginine (Carbon precursors: Glutamate/Glutamine/Proline; Other Precursors: Ammonia, Aspartate) – Cysteine (Carbon precursor: Serine; Other Precursor: Methionine) – Histidine – Tyrosine Reference: J. Nutr. July 1, 2000 vol. 130 no. 7 1835S-1840S, The American Society for Nutritional Sciences • Immunosuppressed patients or those with postoperative infections are often treated with arginine and glutamine supplements. Reference: Am J Physiol Endocrinol Metab. 2011 Aug; 301(2): E264–E266. doi: 10.1152/ajpendo.00223.2011 Powered by TCPDF (www.tcpdf.org) 5 / 5.
Load more

Recommended publications
  • Effect of Peptide Histidine Isoleucine on Water and Electrolyte Transport in the Human Jejunum
    Gut: first published as 10.1136/gut.25.6.624 on 1 June 1984. Downloaded from Gut, 1984, 25, 624-628 Alimentary tract and pancreas Effect of peptide histidine isoleucine on water and electrolyte transport in the human jejunum K J MORIARTY, J E HEGARTY, K TATEMOTO, V MUTT, N D CHRISTOFIDES, S R BLOOM, AND J R WOOD From the Department of Gastroenterology, St Bartholomew's Hospital, London, The Liver Unit, King's College Hospital, London, Department ofMedicine, Hammersmith Hospital, London, and Department of Biochemistry, Karolinska Institute, Stockholm, Sweden SUMMARY Peptide histidine isoleucine, a 27 amino acid peptide with close amino acid sequence homology to vasoactive intestinal peptide and secretin, is distributed throughout the mammalian intestinal tract, where it has been localised to intramural neurones. An intestinal perfusion technique has been used to study the effect of intravenous peptide histidine isoleucine (44.5 pmol/kg/min) on water and electrolyte transport from a plasma like electrolyte solution in human jejunum in vivo. Peptide histidine isoleucine infusion produced peak plasma peptide histidine isoleucine concentrations in the range 2000-3000 pmolIl, flushing, tachycardia and a reduction in diastolic blood pressure. Peptide histidine isoleucine caused a significant inhibition of net absorption of water, sodium, potassium and bicarbonate and induced a net secretion of chloride, these changes being completely reversed during the post-peptide histidine isoleucine period. These findings suggest that endogenous peptide histidine isoleucine may participate in the neurohumoral regulation of water and electrolyte transport in the human jejunum. http://gut.bmj.com/ Peptide histidine isoleucine, isolated originally from INTESTINAL PERFUSION mammalian small intestine, is a 27-amino acid After an eight hour fast, each subject swallowed a peptide having close amino acid sequence homology double lumen intestinal perfusion tube, incorpo- to vasoactive intestinal peptide and secretin.
    [Show full text]
  • Workshop 1 – Biochemistry (Chem 160)
    Workshop 1 – Biochemistry (Chem 160) 1. Draw the following peptide at pH = 7 and make sure to include the overall charge, label the N- and C-terminus, the peptide bond and the -carbon. AVDKY Give the overall charge of the peptide at pH = 3 and 12. 2. Draw a titration curve for Arg, make sure to label the different points. Determine the pI for Arg. 3. Nonpolar solute + water = solution a. What is the S of the universe, system and surroundings? The S of the universe would decrease this is why it is not spontaneous, the S of the system would increase but to a lesser extent to which the S of the surrounding would decrease S universe = S system + S surroundings 4. What is the hydrophobic effect and explain why it is thermodynamically favorable. The hydrophobic effect is when hydrophobic molecules tend to clump together burying them and placing hydrophilic molecules on the outside. The reason this is thermodynamically favorable is because it frees caged water molecules when burying clumping the hydrophobic molecules together. 5. Urea dissolves very readily in water, but the solution becomes very cold as the urea dissolves. How is this possible? Urea dissolves in water because when dissolving there is a net increase in entropy of the universe. The heat exchange, getting colder only reflects the enthalpy (H) component of the total energy change. The entropy change is high enough to offset the enthalpy component and to add up to an overall -G 6. A mutation that changes an alanine residue in the interior of a protein to valine is found to lead to a loss of activity.
    [Show full text]
  • Effects of Single Amino Acid Deficiency on Mrna Translation Are Markedly
    www.nature.com/scientificreports OPEN Efects of single amino acid defciency on mRNA translation are markedly diferent for methionine Received: 12 December 2016 Accepted: 4 May 2018 versus leucine Published: xx xx xxxx Kevin M. Mazor, Leiming Dong, Yuanhui Mao, Robert V. Swanda, Shu-Bing Qian & Martha H. Stipanuk Although amino acids are known regulators of translation, the unique contributions of specifc amino acids are not well understood. We compared efects of culturing HEK293T cells in medium lacking either leucine, methionine, histidine, or arginine on eIF2 and 4EBP1 phosphorylation and measures of mRNA translation. Methionine starvation caused the most drastic decrease in translation as assessed by polysome formation, ribosome profling, and a measure of protein synthesis (puromycin-labeled polypeptides) but had no signifcant efect on eIF2 phosphorylation, 4EBP1 hyperphosphorylation or 4EBP1 binding to eIF4E. Leucine starvation suppressed polysome formation and was the only tested condition that caused a signifcant decrease in 4EBP1 phosphorylation or increase in 4EBP1 binding to eIF4E, but efects of leucine starvation were not replicated by overexpressing nonphosphorylatable 4EBP1. This suggests the binding of 4EBP1 to eIF4E may not by itself explain the suppression of mRNA translation under conditions of leucine starvation. Ribosome profling suggested that leucine deprivation may primarily inhibit ribosome loading, whereas methionine deprivation may primarily impair start site recognition. These data underscore our lack of a full
    [Show full text]
  • Mendelian Randomization Study on Amino Acid Metabolism Suggests Tyrosine As Causal Trait for Type 2 Diabetes
    nutrients Article Mendelian Randomization Study on Amino Acid Metabolism Suggests Tyrosine as Causal Trait for Type 2 Diabetes Susanne Jäger 1,2,* , Rafael Cuadrat 1,2, Clemens Wittenbecher 1,2,3, Anna Floegel 4, Per Hoffmann 5,6, Cornelia Prehn 7 , Jerzy Adamski 2,7,8,9 , Tobias Pischon 10,11,12 and Matthias B. Schulze 1,2,13 1 Department of Molecular Epidemiology, German Institute of Human Nutrition Potsdam-Rehbruecke, 14558 Nuthetal, Germany; [email protected] (R.C.); [email protected] (C.W.); [email protected] (M.B.S.) 2 German Center for Diabetes Research (DZD), 85764 Neuherberg, Germany; [email protected] 3 Department of Nutrition, Harvard T.H. Chan School of Public Health, Boston, MA 02115, USA 4 Leibniz Institute for Prevention Research and Epidemiology-BIPS, 28359 Bremen, Germany; fl[email protected] 5 Human Genomics Research Group, Department of Biomedicine, University of Basel, 4031 Basel, Switzerland; per.hoff[email protected] 6 Institute of Human Genetics, Division of Genomics, Life & Brain Research Centre, University Hospital of Bonn, 53105 Bonn, Germany 7 Research Unit Molecular Endocrinology and Metabolism, Helmholtz Zentrum München, German Research Center for Environmental Health, 85764 Neuherberg, Germany; [email protected] 8 Chair of Experimental Genetics, Center of Life and Food Sciences Weihenstephan, Technische Universität München, 85354 Freising-Weihenstephan, Germany 9 Department of Biochemistry, Yong Loo Lin School of Medicine, National University of Singapore, 8 Medical Drive,
    [Show full text]
  • H-Tyrosine-Glycine-Phenylalanine-Glycine-Glycine-OH for the Treatment of Chronic Idiopathic Myelofibrosis
    European Medicines Agency Pre-authorisation Evaluation of Medicines for Human Use Document Date: London, 5 October 2009 Doc.Ref.: EMEA/COMP/1579/2003 Rev.1 Please note that this product was withdrawn from the Community Register of designated Orphan Medicinal Products in March 2009 on request of the Sponsor. Committee for Orphan Medicinal Products Public summary of positive opinion for orphan designation of H-Tyrosine-Glycine-Phenylalanine-Glycine-Glycine-OH for the treatment of chronic idiopathic myelofibrosis On 20 October 2003, orphan designation (EU/3/03/167) was granted by the European Commission to Abiogen Pharma S.p.A, Italy, for H-Tyrosine-Glycine-Phenylalanine-Glycine-Glycine-OH for the treatment of chronic idiopathic myelofibrosis. What is chronic idiopathic myelofibrosis? Chronic idiopathic myelofibrosis is a disease in which cancer cells are found in the blood and in the bone marrow. The bone marrow is the spongy tissue inside the large bones in the body. Normally the bone marrow makes cells called “blasts” that mature into several different types of blood cells that have specific functions in the body. These include red cells, white cells and platelets. Red blood cells carry oxygen and other materials to all tissues of the body. White blood cells fight infection. Platelets make the blood clot. When myelofibrosis develops, the bone marrow produces large number of abnormal blood cells. In chronic idiopathic myelofibrosis the abnormal population of cells produce substances that alter the growth media of bone marrow and makes bone marrow very dense and rigid. As the abnormal bone marrow environment is no more adequate for the cells, some migrate to other sites where proliferation and maturation take place.
    [Show full text]
  • Amino Acid Recognition by Aminoacyl-Trna Synthetases
    www.nature.com/scientificreports OPEN The structural basis of the genetic code: amino acid recognition by aminoacyl‑tRNA synthetases Florian Kaiser1,2,4*, Sarah Krautwurst3,4, Sebastian Salentin1, V. Joachim Haupt1,2, Christoph Leberecht3, Sebastian Bittrich3, Dirk Labudde3 & Michael Schroeder1 Storage and directed transfer of information is the key requirement for the development of life. Yet any information stored on our genes is useless without its correct interpretation. The genetic code defnes the rule set to decode this information. Aminoacyl-tRNA synthetases are at the heart of this process. We extensively characterize how these enzymes distinguish all natural amino acids based on the computational analysis of crystallographic structure data. The results of this meta-analysis show that the correct read-out of genetic information is a delicate interplay between the composition of the binding site, non-covalent interactions, error correction mechanisms, and steric efects. One of the most profound open questions in biology is how the genetic code was established. While proteins are encoded by nucleic acid blueprints, decoding this information in turn requires proteins. Te emergence of this self-referencing system poses a chicken-or-egg dilemma and its origin is still heavily debated 1,2. Aminoacyl-tRNA synthetases (aaRSs) implement the correct assignment of amino acids to their codons and are thus inherently connected to the emergence of genetic coding. Tese enzymes link tRNA molecules with their amino acid cargo and are consequently vital for protein biosynthesis. Beside the correct recognition of tRNA features3, highly specifc non-covalent interactions in the binding sites of aaRSs are required to correctly detect the designated amino acid4–7 and to prevent errors in biosynthesis5,8.
    [Show full text]
  • Relative Reaction Rates of the Amino Acids Cysteine, Methionine, and Histidine with Analogs of the Anti-Cancer Drug Cisplatin Cynthia A
    Western Kentucky University TopSCHOLAR® Honors College Capstone Experience/Thesis Honors College at WKU Projects 5-11-2015 Relative Reaction Rates of the Amino Acids Cysteine, Methionine, and Histidine with Analogs of the Anti-Cancer Drug Cisplatin Cynthia A. Tope Western Kentucky University, [email protected] Follow this and additional works at: http://digitalcommons.wku.edu/stu_hon_theses Part of the Medicinal-Pharmaceutical Chemistry Commons Recommended Citation Tope, Cynthia A., "Relative Reaction Rates of the Amino Acids Cysteine, Methionine, and Histidine with Analogs of the Anti-Cancer Drug Cisplatin" (2015). Honors College Capstone Experience/Thesis Projects. Paper 571. http://digitalcommons.wku.edu/stu_hon_theses/571 This Thesis is brought to you for free and open access by TopSCHOLAR®. It has been accepted for inclusion in Honors College Capstone Experience/ Thesis Projects by an authorized administrator of TopSCHOLAR®. For more information, please contact [email protected]. RELATIVE REACTION RATES OF THE AMINO ACIDS CYSTEINE, METHIONINE, AND HISTIDINE WITH ANALOGS OF THE ANTI-CANCER DRUG CISPLATIN A Capstone Experience/Thesis Project Presented in Partial Fulfillment of the Requirements for the Degree Bachelor of Science with Honors College Graduate Distinction at Western Kentucky University By: Cynthia A. Tope ***** Western Kentucky University 2015 CE/T Committee: Approved by: Professor Kevin Williams, Advisor _________________________ Professor Darwin Dahl Advisor Professor Lee Ann Smith Department of Chemistry Copyright: Cynthia A. Tope 2015 ABSTRACT We are studying the reaction of analogs of the anticancer drug cisplatin with amino acids that differ in size and shape. The reaction of cisplatin with proteins likely precedes reaction with DNA in the body, forming a variety of products that may be toxic to the human body.
    [Show full text]
  • Effects of Basic Amino Acids and Their Derivatives on SARS-Cov-2 and Influenza-A Virus Infection
    viruses Article Effects of Basic Amino Acids and Their Derivatives on SARS-CoV-2 and Influenza-A Virus Infection Ivonne Melano 1 , Li-Lan Kuo 2, Yan-Chung Lo 3, Po-Wei Sung 4, Ni Tien 5,6 and Wen-Chi Su 1,2,7,* 1 Graduate Institute of Biomedical Sciences, College of Medicine, China Medical University, Taichung 40402, Taiwan; [email protected] 2 Research Center for Emerging Viruses, China Medical University Hospital, Taichung 40402, Taiwan; [email protected] 3 Sinphar Pharmaceutical Co., Ltd., Sinphar Group, Yilan 269, Taiwan; [email protected] 4 School of Medicine, China Medical University, Taichung 40402, Taiwan; [email protected] 5 Department of Laboratory Medicine, China Medical University Hospital, Taichung 40402, Taiwan; [email protected] 6 Department of Medical Laboratory Science and Biotechnology, China Medical University, Taichung 40402, Taiwan 7 International Master’s Program of Biomedical Sciences, China Medical University, Taichung 40402, Taiwan * Correspondence: [email protected] Abstract: Amino acids have been implicated with virus infection and replication. Here, we demon- strate the effects of two basic amino acids, arginine and lysine, and their ester derivatives on infection of two enveloped viruses, SARS-CoV-2, and influenza A virus. We found that lysine and its ester derivative can efficiently block infection of both viruses in vitro. Furthermore, the arginine ester derivative caused a significant boost in virus infection. Studies on their mechanism of action revealed that the compounds potentially disturb virus uncoating rather than virus attachment and endosomal Citation: Melano, I.; Kuo, L.-L.; Lo, acidification. Our findings suggest that lysine supplementation and the reduction of arginine-rich Y.-C.; Sung, P.-W.; Tien, N.; Su, W.-C.
    [Show full text]
  • Electrochemical Studies of Dl-Leucine, L-Proline and L
    ELECTROCHEMICAL STUDIES OF DL -LEUCINE, 60 L-PROLINE AND L-TRYPTOPHAN AND THEIR INTERACTION WITH COPPER AND IRON 30 c b A) M. A. Jabbar, R. J. Mannan, S. Salauddin and B. µ a Rashid 0 Department of Chemistry, University of Dhaka, ( Current Dhaka-1000, Bangladesh -30 Introduction -60 In vitro study of the charge transfer reactions coupled -800 -400 0 400 800 with chemical reactions can give important indication of Potential vs. Ag/AgCl (mV) about actual biological processes occurring in human Fig.1. Comparison of the cyclic voltammogram of system. Understanding of such charge-transfer 5.0mM (a) DL -Leucine, (b) Cu-DL -Leucine ion and mechanism will help to determine the effectiveness of (c) [Fe-DL -Leucine] in 0.1M KCl solution at a Pt- nutrition, metabolism and treatment of various biological button electrode. Scan rates 50 mV/s. disorders. In the previous research, the redox behaviour of 40 various amino acids and biochemically important compounds and their charge transfer reaction and their b interaction of metal ions were studied [1,2]. In the present 20 ) a c research, the redox behavior and the charge transfer µΑ kinetics of DL -Leucine, L-Proline and L-Tryptophan in 0 the presence and absence of copper and iron will be investigated. Current ( -20 Experimental A computerized electrochemistry system developed by -40 -800 -400 0 400 800 Advanced Analytics, Virginia, USA, (Model-2040) Potential vs. Ag/AgCl (mV) consisting of three electrodes micro-cell with a saturated Ag/AgCl reference, a Pt-wire auxiliary and a pretreated Fig.2 . Comparison of the cyclic voltammogram of Pt-button working electrode is employed to investigate 5.0mM (a) L-Proline, (b) Cu-L-Proline and (c) Fe-L- Proline in 0.1M KCl solution at a Pt-button different amino acids and metal-amino acid systems.
    [Show full text]
  • Convenient Preparation of Poly(L-Histidine) by the Direct Polymerization of L-Histidine Or Nim Benzyl-L-Histidine with Diphenylphosphoryl Azide
    Polymer Journal, Vol. 13, No. 12, pp 1151-1154 (1981) SHORT COMMUNICATION Convenient Preparation of Poly(L-histidine) by the Direct Polymerization of L-Histidine or Nim_Benzyl-L-histidine with Diphenylphosphoryl Azide Takumi NARUSE, Bun-ichiro NAKAJIMA, Akihiro TSUTSUMI, and Norio NISHI Department of Polymer Science, Faculty of Science, Hokkaido University, Nishi 8-chome, Kita 10-jo, Kita-ku, Sapporo 060, Japan. (Received August 14, 1981) KEY WORDS Polymerization I Diphenylphosphoryl Azide (DPPA) I L- Histidine I N'm-Benzyl-L-histidine I Poly(L-histidine) I Poly(N'm-benzyl-L­ histidine) I IR Spectrum I 13C NMR Spectrum I Intrinsic Viscosity I Poly(L-histidine) is a very interesting poly(a­ histidine) by the polymerization of L-histidine with amino acid) as a synthetic functional polymer or as iodine-phosphonic acid esters was unsuccessful. The a model for the functional biopolymer such as simplification of the synthetic route for poly(L­ enzymes. It is known, however, that poly(L­ histidine) is still necessary. histidine) can not be prepared by the Fuchs­ Diphenylphosphoryl azide (DPPA) has been used Farthing method 1 which is very popular for prepar­ as a convenient reagent for racemization-free pep­ ing poly(a-amino acid)s. A synthetic route with tide synthesis, since it was synthesized by Shioiri et several steps involving the synthesis of NCA (a­ a!. in 1972.6 Recently, we reported that this reagent amino acid N-carboxyanhydride) by the rather can also be used successfully for the polymerization classical Leuchs method/ have been used for the of amino acids or peptides.
    [Show full text]
  • Enhancing Effect of Glycine and Tryptophan Mixture on Estimated
    Functional Foods in Health and Disease 2021; 11(1): 24-33 www.ffhdj.com Page 24 of 33 Research Article Open Access Enhancing effect of glycine and tryptophan mixture on estimated glomerular filtration rate in healthy participants: A randomized, double-blind, placebo-controlled parallel study Shunji Oshima*, Sachie Shiiya, Yasunori Nakamura Core Technology Laboratories, Asahi Quality and Innovations, Ltd., Ibaraki, Japan *Corresponding author: Shunji Oshima, PhD, Core Technology Laboratories, Asahi Quality & Innovations, Ltd., 1-21, Midori 1-chome, Moriya-shi, Ibaraki, 302-0106, Japan. Submission Date: January 7th, 2021; Acceptance Date: January 22nd, 2021; Publication Date: January 29th, 2021 Please cite this article as: Oshima S., Shiiya S., Nakamura Y. Enhancing effect of glycine and tryptophan mixture on estimated glomerular filtration rate in healthy participants: A randomized, double-blind, placebo-controlled parallel study. Functional Foods in Health and Disease 2021. 11(1): 24-33. DOI: https://www.doi.org/10.31989/ffhd.v11i1.774 ABSTRACT Background: The mixture of glycine and tryptophan exhibited serum uric acid-lowering effects in our previous clinical trial. Objective: Using a randomized, double-blind, placebo- controlled, and parallel study design, this current study aimed to examine whether this mixture enhanced the estimated glomerular filtration rate (eGFR) as an indicator of renal function in healthy individuals. Methods: Healthy Japanese adult males and females ingested a powder mixture containing 3.0 g of glycine and 0.2 g of tryptophan or a placebo powder once daily at bedtime for 8 weeks. Results: After 8 weeks of continual ingestion, the combined glycine and tryptophan supplementation significantly enhanced eGFR.
    [Show full text]
  • Amino Acids Amino Acids
    Amino Acids Amino Acids What Are Amino Acids? Essential Amino Acids Non Essential Amino Acids Amino acids are the building blocks of proteins; proteins are made of amino acids. Isoleucine Arginine (conditional) When you ingest a protein your body breaks it down into the individual aminos, Leucine Glutamine (conditional) reorders them, re-folds them, and turns them into whatever is needed by the body at Lysine Tyrosine (conditional) that time. From only 20 amino acids, the body is able to make thousands of unique proteins with different functions. Methionine Cysteine (conditional) Phenylalanine Glycine (conditional) Threonine Proline (conditional) Did You Know? Tryptophan Serine (conditional) Valine Ornithine (conditional) There are 20 different types of amino acids that can be combined to make a protein. Each protein consists of 50 to 2,000 amino acids that are connected together in a specific Histidine* Alanine sequence. The sequence of the amino acids determines each protein’s unique structure Asparagine and its specific function in the body. Asparate Popular Amino Acid Supplements How Do They Benefit Our Health? Acetyl L- Carnitine: As part of its role in supporting L-Lysine: L-Lysine, an essential amino acid, is mental function, Acetyl L-Carnitine may help needed to support proper growth and bone Proteins (amino acids) are needed by your body to maintain muscles, bones, blood, as support memory, attention span and mental development. It can also support immune function. well as create enzymes, neurotransmitters and antibodies, as well as transport and performance. store molecules. N-Acetyl Cysteine: N-Acetyl Cysteine (NAC) is a L-Arginine: L-Arginine is a nonessential amino acid form of the amino acid cysteine.
    [Show full text]