L-Methionine
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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 -
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. -
Impact of Steam Treatment on Protein Quality Indicators of Full Fat Soybeans from Different Origins
Impact of steam treatment on protein quality indicators of full fat soybeans from different origins Pieter Bos 20-10-2019 1 Wageningen University ASG - Animal Nutrition Group Impact of steam treatment on protein quality indicators of full fat soybeans from different origins Author : Bos, P. Registration nr. : 940221104030 Code : ANU-80436 Supervisor(s) : A.F.B. van der Poel, G. Bosch Wageningen, Oktober 2018 2 Copyright Niets uit dit verslag mag worden verveelvoudigd en/of openbaar gemaakt door middel van druk, fotokopie, microfilm of welke andere wijze ook, zonder voorafgaande schriftelijke toestemming van de hoogleraar van de leerstoelgroep Diervoeding van Wageningen Universiteit. No part of this publication may be reproduced or published in any form or by any means, electronic, mechanical, photocopying, recording or otherwise, without prior written permission of the head of the Animal Nutrition Group of Wageningen University, The Netherlands. 3 Summary The production of soybeans in the EU-28 in 2016 was 2.4 million tons, which is only 0.7% of the global production. From a social perspective, there is a stimulus in the Netherlands to a protein transition in which regional proteins are used for livestock farming. Heat-treated full-fat soybeans (FFSB) can be an important protein source. Due to the gap in knowledge about European soybeans, more research can provide clarity about protein quality of European FFSB. In this study, raw GMO- free, unprocessed soybeans from European zone (France, FFSBFR; Netherlands, FFSBNL ) and common used beans (Ukraine, FFSBUKR; Brazil, FFSBBR) were steam-toasted for 9 different time- temperature combinations, and analysed on different in-vitro protein quality indicators: Trypsin inhibitor activity (TIA), total and reactive lysine (rLys, tLys), crude protein (CP), pH-stat digestibility at 10 minutes (DH10) and 120 minutes (DH120), and protein dispersibility index (PDI). -
Breeding for Quality Protein Maize (QPM) Varieties: a Review
agronomy Review Breeding for Quality Protein Maize (QPM) Varieties: A Review Liliane N. Tandzi 1,2,*, Charles S. Mutengwa 1, Eddy L. M. Ngonkeu 2,3, Noé Woïn 2 and Vernon Gracen 4 1 Department of Agronomy, Faculty of Science and Agriculture, University of Fort Hare, P. Bag X1314, Alice 5700, South Africa; [email protected] 2 Institute of Agricultural Research for Development (IRAD), P.O. Box 2123, Messa, Yaounde, Cameroon; [email protected] (E.L.M.N.); [email protected] (N.W.) 3 Department of Plant Biology and Physiology, Faculty of Science, University of Yaounde I, Yaounde, Cameroon 4 West Africa Centre for Crop Improvement (WACCI), College of Basic and Applied Sciences, University of Ghana, Legon PMB LG 30, Accra 999064, Ghana; [email protected] * Correspondence: [email protected] or [email protected]; Tel.: +27-063-459-4323 Received: 28 August 2017; Accepted: 19 October 2017; Published: 28 November 2017 Abstract: The nutritional evaluation of quality protein maize (QPM) in feeding trials has proved its nutritional superiority over non-QPM varieties for human and livestock consumption. The present paper reviews some of the most recent achievements in development of QPM varieties using both conventional and molecular breeding under stressed and non-stressed environments. It is evident that numerous QPM varieties have been developed and released around the world over the past few decades. While the review points out some gaps in information or research efforts, challenges associated with adoption QPM varieties are highlighted and suggestions to overcome them are presented. The adoption of released varieties and challenges facing QPM production at the farmer level are also mentioned. -
Egg Consumption and Human Health
nutrients Egg Consumption and Human Health Edited by Maria Luz Fernandez Printed Edition of the Special Issue Published in Nutrients www.mdpi.com/journal/nutrients Egg Consumption and Human Health Special Issue Editor Maria Luz Fernandez MDPI • Basel • Beijing • Wuhan • Barcelona • Belgrade Special Issue Editor Maria Luz Fernandez University of Connecticut USA Editorial Office MDPI AG St. Alban-Anlage 66 Basel, Switzerland This edition is a reprint of the Special Issue published online in the open access journal Nutrients (ISSN 2072-6643) in 2015–2016 (available at: http://www.mdpi.com/journal/nutrients/special issues/egg-consumption-human-health). For citation purposes, cite each article independently as indicated on the article page online and as indicated below: Lastname, F.M.; Lastname, F.M. Article title. Journal Name. Year. Article number, page range. First Edition 2018 ISBN 978-3-03842-666-0 (Pbk) ISBN 978-3-03842-667-7 (PDF) Articles in this volume are Open Access and distributed under the Creative Commons Attribution (CC BY) license, which allows users to download, copy and build upon published articles even for commercial purposes, as long as the author and publisher are properly credited, which ensures maximum dissemination and a wider impact of our publications. The book taken as a whole is c 2018 MDPI, Basel, Switzerland, distributed under the terms and conditions of the Creative Commons license CC BY-NC-ND (http://creativecommons.org/licenses/by-nc-nd/4.0/). Table of Contents About the Special Issue Editor ...................................... v Preface to ”Egg Consumption and Human Health” .......................... vii Jose M. Miranda, Xaquin Anton, Celia Redondo-Valbuena, Paula Roca-Saavedra, Jose A. -
Methionine Livestock
National Organic Standards Board Technical Advisory Panel Review for the USDA National Organic Program May 21, 2001 Methionine Livestock 1 Executive Summary 2 3 The NOSB received a petition in 1995 to add all synthetic amino acids to the National List. After deliberation of a 4 review prepared by the TAP in 1996 and 1999, the NOSB requested a case-by-case review of synthetic amino acids used 5 in livestock production, and referred three forms of methionine to the TAP. 6 7 All of the TAP reviewers found these three forms to be synthetic. Two TAP reviewers advised that synthetic methionine 8 remain prohibited. The one reviewer who advises the NOSB to recommend adding synthetic methionine to the National 9 List agrees that it is not compatible with organic principles and suggests limitations on its use until non-synthetic sources 10 are more widely available. 11 12 The majority of the reviewers advise the NOSB to not add them to the National List for the following reasons: 13 1) Adequate organic and natural sources of protein are available [§6517(c)(1)(A)(ii)]; 14 2) Methionine supplementation is primarily to increase growth and production, not to maintain bird health, and 15 this is counter to principles embodied in the OFPA requirements for organic feed [§6509(c)(1)]; 16 3) Pure amino acids in general and synthetic forms of methionine in particular are not compatible with a 17 sustainable, whole-systems approach to animal nutrition and nutrient cycling [§6518(m)(7)]. 18 19 Methionine is an essential amino acid needed for healthy and productive poultry. -
Sports Nutrition: a Review of Selected Nutritional Supplements for Bodybuilders and Strength Athletes
Sports Nutrition: A Review of Selected Nutritional Supplements For Bodybuilders and Strength Athletes Gregory S. Kelly, N.D. Abstract Because there is widespread belief among athletes that special nutritional practices will enhance their achievements in competition, the use of supplements has become common. Accompanying the growth in supplementation by athletes has been a corresponding increase in exaggerated claims or misleading information. This article reviews several supplements currently popular among bodybuilders and other strength athletes in order to clarify which products can be expected to produce results. Included in the discussion are creatine monohydrate, beta-hydroxy beta-methylbutyrate, whey protein, phosphatidylserine, and selected amino acids and minerals. (Alt Med Rev 1997; 2(3):184-201) Introduction The increased focus on fitness and subsequent research in the exercise field has ex- panded the role of nutrition as it relates to sports performance. Because there is widespread belief among athletes that special nutritional practices will enhance their achievements in com- petition, the use of supplements has become common. Although some of the supplements have proven benefits, historically a great deal of the information on products is either misleading or exaggerated. This is perhaps best witnessed in the products marketed to bodybuilders and other athletes concerned with size, strength, and body composition. This article reviews some of the supplements currently promoted in this market in an effort to determine which contribute to maximizing results. Included in the review are creatine monohydrate, beta-hydroxy beta- methylbutyrate (HMB), whey protein, phosphatidylserine, and selected amino acids and minerals. Creatine Monohydrate Creatine monohydrate has become one of the most popular supplements in the history of bodybuilding. -
Amino Acid Transport Pathways in the Small Intestine of the Neonatal Rat
Pediat. Res. 6: 713-719 (1972) Amino acid neonate intestine transport, amino acid Amino Acid Transport Pathways in the Small Intestine of the Neonatal Rat J. F. FITZGERALD1431, S. REISER, AND P. A. CHRISTIANSEN Departments of Pediatrics, Medicine, and Biochemistry, and Gastrointestinal Research Laboratory, Indiana University School of Medicine and Veterans Administration Hospital, Indianapolis, Indiana, USA Extract The activity of amino acid transport pathways in the small intestine of the 2-day-old rat was investigated. Transport was determined by measuring the uptake of 1 mM con- centrations of various amino acids by intestinal segments after a 5- or 10-min incuba- tion and it was expressed as intracellular accumulation. The neutral amino acid transport pathway was well developed with intracellular accumulation values for leucine, isoleucine, valine, methionine, tryptophan, phenyl- alanine, tyrosine, and alanine ranging from 3.9-5.6 mM/5 min. The intracellular accumulation of the hydroxy-containing neutral amino acids threonine (essential) and serine (nonessential) were 2.7 mM/5 min, a value significantly lower than those of the other neutral amino acids. The accumulation of histidine was also well below the level for the other neutral amino acids (1.9 mM/5 min). The basic amino acid transport pathway was also operational with accumulation values for lysine, arginine and ornithine ranging from 1.7-2.0 mM/5 min. Accumulation of the essential amino acid lysine was not statistically different from that of nonessential ornithine. Ac- cumulation of aspartic and glutamic acid was only 0.24-0.28 mM/5 min indicating a very low activity of the acidic amino acid transport pathway. -
U.S. Dairy Proteins: High-Quality and Complete Protein Sources
Role: Name: Initials: Date: Order Role: Name: Initials: Date: Order: Deadlines Proofing Laura GCD Internal: Producer Courtney Art Buyer Client: Print/Ship: Writer Account Exec. BW’s to: Art Director Emily Senior Level AE Colors to: PDF to: ACD Other Package to: Production Lead Jeff Other 1 2 3 4 5 6 7 Production Artist Ashley Other 8 9 10 11 12 Nutrition Spotlight: U.S. Dairy Proteins: High-quality and Complete Protein Sources All dairy foods and ingredients start out as milk, which contains 3.5 percent protein — 80 percent casein and 20 percent whey. Milk protein ingredients contain the same protein ratio found in milk, while whey protein ingredients contain 100 percent whey. U.S. dairy proteins with protein levels 80 percent and higher are widely used in health and wellness and sports nutrition products. Benefits of Dairy Protein Published nutrition research on the health and nutritional benefits of dairy proteins continues to rise each year, supporting the benefits of incorporating whey and milk proteins into the daily diet. Protein is an essential nutrient the body needs to build and maintain muscle. Protein also plays an integral role in the body's structure, functions and regulation of all tissues and organs. There are many health and wellness benefits for all types of lifestyles that come from eating U.S. dairy proteins. Research shows that1-18 diets higher in protein help slow muscle loss, curb hunger, maintain a healthy weight, build lean muscle (with regular resistance exercise) and enhance exercise recovery. DID YOU KNOW nn U.S. dairy proteins score at or near the top in current methods used to measure protein quality. -
Dietary Protein Quality Evaluation in Human Nutrition: Report of an FAO Expert Consultation
ISSN 0254-4725 FAO Dietary protein quality FOOD AND NUTRITION evaluation in human PAPER nutrition 92 Report of an FAO Expert Consultation FAO Dietary protein quality FOOD AND NUTRITION evaluation in PAPER human nutrition 92 Report of an FAO Expert Consultation 31 March–2 April, 2011 Auckland, New Zealand FOOD AND AGRICULTURE ORGANIZATION OF THE UNITED NATIONS ROME, 2013 The designations employed and the presentation of material in this information product do not imply the expression of any opinion whatsoever on the part of the Food and Agriculture Organization of the United Nations (FAO) concerning the legal or development status of any country, territory, city or area or of its authorities, or concerning the delimitation of its frontiers or boundaries. The mention of specific companies or products of manufacturers, whether or not these have been patented, does not imply that these have been endorsed or recommended by FAO in preference to others of a similar nature that are not mentioned. The views expressed in this information product are those of the author(s) and do not necessarily reflect the views of FAO. ISBN 978-92-5-107417-6 All rights reserved. FAO encourages reproduction and dissemination of material in this information product. Non-commercial uses will be authorized free of charge, upon request. Reproduction for resale or other commercial purposes, including educational purposes, may incur fees. Applications for permission to reproduce or disseminate FAO copyright materials, and all queries concerning rights and licences, should be addressed by e-mail to [email protected] or to the Chief, Publishing Policy and Support Branch, Office of Knowledge Exchange, Research and Extension, FAO, Viale delle Terme di Caracalla, 00153 Rome, Italy. -
Amino Acid Degradation
BI/CH 422/622 OUTLINE: OUTLINE: Protein Degradation (Catabolism) Digestion Amino-Acid Degradation Inside of cells Protein turnover Dealing with the carbon Ubiquitin Fates of the 29 Activation-E1 Seven Families Conjugation-E2 nitrogen atoms in 20 1. ADENQ Ligation-E3 AA: Proteosome 2. RPH 9 ammonia oxidase Amino-Acid Degradation 18 transamination Ammonia 2 urea one-carbon metabolism free transamination-mechanism to know THF Urea Cycle – dealing with the nitrogen SAM 5 Steps Carbamoyl-phosphate synthetase 3. GSC Ornithine transcarbamylase PLP uses Arginino-succinate synthetase Arginino-succinase 4. MT – one carbon metabolism Arginase 5. FY – oxidase vs oxygenase Energetics Urea Bi-cycle 6. KW – Urea Cycle – dealing with the nitrogen 7. BCAA – VIL Feeding the Urea Cycle Glucose-Alanine Cycle Convergence with Fatty acid-odd chain Free Ammonia Overview Glutamine Glutamate dehydrogenase Overall energetics Amino Acid A. Concepts 1. ConvergentDegradation 2. ketogenic/glucogenic 3. Reactions seen before The SEVEN (7) Families B. Transaminase (A,D,E) / Deaminase (Q,N) Family C. Related to biosynthesis (R,P,H; C,G,S; M,T) 1.Glu Family a. Introduce oxidases/oxygenases b. Introduce one-carbon metabolism (1C) 2.Pyruvate Family a. PLP reactions 3. a-Ketobutyric Family (M,T) a. 1-C metabolism D. Dedicated 1. Aromatic Family (F,Y) a. oxidases/oxygenases 2. a-Ketoadipic Family (K,W) 3. Branched-chain Family (V,I,L) E. Convergence with Fatty Acids: propionyl-CoA 29 N 1 Amino Acid Degradation • Intermediates of the central metabolic pathway • Some amino acids result in more than one intermediate. • Ketogenic amino acids can be converted to ketone bodies. -
Where Metal Ions Bind in Proteins (Metafloprotein/Protein Structure/Hydrophobicity Contrast Function) MASON M
Proc. Nadl. Acad. Sci. USA Vol. 87, pp. 5648-5652, August 1990 Biophysics Where metal ions bind in proteins (metafloprotein/protein structure/hydrophobicity contrast function) MASON M. YAMASHITA*t, LAURA WESSON*, GEORGE EISENMANt, AND DAVID EISENBERG*§ *Molecular Biology Institute and Department of Chemistry and Biochemistry, and *Department of Physiology, University of California, Los Angeles, CA 90024 Contributed by David Eisenberg, May 14, 1990 ABSTRACT The environments of metal ions (Li', Na', K+, Ag+, Cs+, Mg2+, Ca2+, Mn2+9 Cu2+, Zn2+) in proteins and other metal-host molecules have been examined. Regard- .. 0.00- ______ less ofthe metal and its precise pattern ofligation to the protein, there is a common qualitative feature to the bind site: the metal is ligated by a shell of hydrophilic atomic groups (con- E -0.01 Zn2+ taining oxygen, nitrogen, or sulfur atoms) and this hydrophilic shell is embedded within a larger shell of hydrophobic atomic - -0.02 groups (containing carbon atoms). That is, metals bind at centers of high hydrophobicity contrast. This qualitative ob- servation can be described analytically by the hydrophobicity 0 2 4 6 8 10 contrast function, C, evaluated from the structure. This func- tion is large and positive for a sphere of hydrophilic atomic 0.01 groups (characterized by atomic salvation parameters, Aar, having values < 0) at the center of a larger sphere of hydro- phobic atomic groups (characterized by Aor > 0). In the 23 0.00. metal-binding molecules we have examined, the maximum values of the contrast function lie near to observed metal binding sites. This suggests that the hydrophobicity contrast function may be useful for locating, characterizing, and de- - -0.01 signing metal binding sites in proteins.