DOCSLIB.ORG

Us 2018 / 0362598 A1

Total Page：16

File Type：pdf, Size：1020Kb

Download full-text PDF Read full-text
Us 2018 / 0362598 A1 US 20180362598A1 ( 19) United States ( 12) Patent Application Publication (10 ) Pub . No. : US 2018 /0362598 A1 CARLSON et al. ( 43 ) Pub . Date: Dec . 20 , 2018 ( 54 ) CLEAVABLE PEPTIDES AND INSECTICIDAL CO7K 5 / 103 ( 2006 .01 ) AND NEMATICIDAL PROTEINS CO7K 14 /435 (2006 .01 ) COMPRISING SAME CO7K 14 /325 ( 2006 .01 ) (71 ) Applicant: VESTARON CORPORATION , A01N 63 /02 ( 2006 .01 ) KALAMAZOO , MI (US ) C12N 15 /82 (2006 .01 ) (72 ) Inventors : ALVAR R . CARLSON , (52 ) U . S . CI. KALAMAZOO , MI (US ) ; CPC . .. .. CO7K 14 /415 (2013 .01 ) ; CO7K 7 / 06 ALEXANDRA M . HAASE , MARTIN , (2013 .01 ) ; CO7K 5 / 101 ( 2013. 01 ) ; CO7K MI (US ) ; ROBERT M . KENNEDY , 14 / 43518 (2013 .01 ) ; CO7K 14 / 325 (2013 . 01 ) ; DEXTER , MI (US ) CO7K 2319 / 04 ( 2013 .01 ) ; C12N 15 /8285 ( 2013 . 01 ) ; C12N 15 /8286 ( 2013 .01 ) ; COZK ( 73 ) Assignee : VESTARON CORPORATION , 2319 /50 (2013 .01 ) ; CO7K 2319 /55 (2013 .01 ) ; KALAMAZOO , MI (US ) A01N 63 / 02 (2013 .01 ) ( 21 ) Appl. No. : 15 /727 , 277 ( 22 ) Filed : Oct . 6 , 2017 (57 ) ABSTRACT Related U . S . Application Data A peptide comprised of either a binary or a tertiary peptide, (60 ) Provisional application No. 62 /411 , 117 , filed on Oct. the peptide contains at least 4 amino acids and up to a 21 , 2016 . maximum of 16 amino acids, comprised of 2 or 3 different regions, wherein the binary peptides have 2 different regions Publication Classification and the tertiary peptides have 3 different regions; wherein , (51 ) Int . Cl. the peptide can be cleaved by both an animal gut protease CO7K 14 /415 ( 2006 .01 ) and an insect or nematode gut protease . CO7K 7 / 06 ( 2006 .01 ) Specification includes a Sequence Listing . Protease - Quenches State Cleavage Assay Protease cleavage Cleaviige activity occurs blocked Excitable Fluorescence No Change A Variable Amino Acid grid pattern ) Glycine linker (horizontal line pattern : ???? Danor quenched due to proximity of quencher Excited donos søt quenched Patent Application Publication Dec. 20 , 2018 Sheet 1 of 9 US 2018 /0362598 A1 Protease .. Cleavage Assay Protease cleavage Y99 . occurs not " 2 . Excitable Fluorescence Variable Amino Acid ( grid pattern ) Quencher Donor quenched due to proximity of quencher Excited donor not quenched Patent Application Publication Dec . 20 , 2018 Sheet 2 of 9 US 2018 /0362598 A1 ' first aspect ' LL M View second aspect , LAVA the www F M eet * * * * VVV YYY wWA WAMA VAI YYYY ver www qolalarimera WA WY RRRR VUVUVUVUVUVI FIG . 2 Patent Application Publication Dec . 20 , 2018 Sheet 3 of 9 US 2018 /0362598 A1 STA [ TP > V AAAAA WWW4444444 FIG . 3A TP inactive T P active V FIG . 3B Patent Application Publication Dec . 20 , 2018 Sheet 4 of 9 US 2018 /0362598 A1 rrrrrrrrrrrrrrrrrrrrrrrrrrrr ., terreny R. W Y ' ' ' ' ' ' ' ' ' ' wer YYYYYYYYYYYYYY AAAAAAAA Syy wwwwwwwwwww deeeeeeeeee Seeeeeeeeeeeeee esii * AK. * ENNI ww celebele Pyyyyyy veelveleeeeeee V wwwwwwww FIG . 4 Patent Application Publication Dec . 20 , 2018 Sheet 5 of 9 US 2018 /0362598 A1 - - - - - - - - - - - - - - eve seg WAAAAAA w www STA TP yyyyyyyyyyyyyyy zezezeze YYYYYYYYYYY wwwwwwwwwwww VVVV avviveveuwe FIG . 5 Patent Application Publication Dec . 20 , 2018 Sheet 6 of 9 US 2018 /0362598 A1 wwwwwwwwwwwwwwwwwwwwwwwwww . wwwwwwwwwwwwwwwwwwwwwww. w w . angaagaagaagaagaagaa 10H www T B n on an internationalW and intention MMMMMMMMMMMMMMMMMMMMMMMMMM I FIG . 6A U - ACTX -hvia 10H * * * * * * * * * * * * * * * * * * * * * * * * * * * * * * * * * * * * * * * * * * * * * * * * * * * * FIG . 6B FIG . 6C Patent Application Publication Dec. 20 , 2018 Sheet 7 of 9 US 2018 /0362598 A1 Enzyme: SCR Gut extract ALKLFVGS IFVRLRGS 30 210 0 30 210 0 30 210 Enzyme: CEW Gut extract ALKLFVGS FVRLRGS 30 210 0 30 210 0 30 210 Enzyme: SGF ALKLFVGS FVRLRGS IGER 19111111111 0 2 10 0 2 10 0 2 210 FIG . 7 Patent Application Publication Dec. 20 , 2018 Sheet 8 of 9 US 2018 / 0362598 A1 " . ? 1 : ELLA“ ??????: Patent Application Publication Dec. 20 , 2018 Sheet 9 of 9 US 2018 /0362598 A1 DamageScore 77777777777777777777777777777777777777777 FIG . 9 US 2018 /0362598 A1 Dec. 20 , 2018 CLEAVABLE PEPTIDES AND INSECTICIDAL [ 0007 ] Bt proteins, or Bt peptides , are effective insecti AND NEMATICIDAL PROTEINS cides used for crop protection in the form of both plant COMPRISING SAME incorporated protectants and foliar sprays . Commercial for mulations of Bt proteins are widely used to control insects CROSS REFERENCE TO RELATED at the larval stage . Inhibitory cysteine knot motif ( ICK ) APPLICATIONS proteins are also a class of insecticidal peptides which are derived from arthropod origins , such as the venoms of [0001 ] This application claims the benefit of, and priority scorpions or spiders . to , U . S . Provisional Application Ser. No . 62 /411 , 117 , filed [ 0008 ] Other classes and types of potential peptides have on Oct. 21 , 2016 , the disclosure of which is incorporated by been identified , such as Trypsin modulating oostatic factor reference herein in its entirety . ( TMOF ) peptides. TMOF peptides have to be delivered to their physiological site of action for insecticidal activity to SEQUENCE LISTING ensue . TMOF peptides have been identified as potential 10002 ] This application incorporates by reference in its larvicides, with great potential , see D . Borovsky , Journal of entirety the Sequence Listing entitled “ FAM _ O _ US _ Experimental Biology 206 , 3869 - 3875 , but like nearly all 225312 _ 419533 _ SEQ _ LIST_ 2017 _ 10 _ 06 _ ST25. txt” ( 5 .37 other insecticidal peptides , TMOF has not been commer MB ) , which was created on Oct. 6 , 2017 , and filed elec cialized or widely used by farmers and there are reasons for tronically herewith .” this . [ 0009 ] The ability to successfully produce insecticidal FIELD OF THE INVENTION peptides on a commercial scale , with reproducible peptide formation and folding , at a reasonable and economical price , [0003 ] New insecticidal and nematicidal proteins , cleav can be a significant obstacle to commercialization . The wide able peptides, DNA constructs encoding same, transgenic variety , unique properties and special nature of insecticidal proteins , their expression in plants, methods of producing peptides , combined with the huge variety of possible pro the transgenic proteins, new processes , production tech duction techniques, can present an overwhelming number of niques , new peptides, new formulations, and combinations approaches to peptide application and production , but few , if of new and known insecticidal and nematicidal proteins any, are commercially successful. contained within transgenic proteins that produce greater [0010 ] There are several reasons why so few of the mul pest resistance than would be expected of related insecticidal titude insecticidal peptides that have been identified have and nematicidal proteins for the control of insects and ever made it to market . First, most insecticidal peptides are nematodes are described and claimed . either too delicate or not toxic enough to be used commer cially. Second , insecticidal peptides are difficult and costly BACKGROUND to produce commercially . Third , many insecticidal peptides [0004 ] The global security of food produced by modern quickly degrade and have a short half -life . Fourth , very few agriculture and horticulture is challenged by insect pests . insecticidal peptides fold properly when then are expressed Farmers rely on insecticides to suppress insect damage, yet by a plant, thus they lose their toxicity in genetically commercial options for safe and functional insecticides modified organisms (GMOs ) such as genetically modified available to farmers are diminishing through the removal of plants . Fifth , most of the identified insecticidal peptides are dangerous chemicals from the marketplace and the evolution blocked from systemic distribution in the insect and / or lose of insect strains that are resistant to all major classes of their toxic nature when consumed by insects . Bt proteins are chemical and biological insecticides . New insecticides are an exception to this last problem and because they disrupt necessary for farmers to maintain crop protection . insect feeding they have been widely used . [ 0005 ] Insecticidal and nematicidal peptides, polypeptides [0011 ] The present invention provides several solutions to and proteins are peptide and protein polymers that are toxic these major problems which have prevented commercial to their targets , usually insects or nematodes . The insecti ization and wide spread use of insecticidal peptides. The cidal peptides or toxins commonly derive from arthropod present invention provides transgenic proteins that enable origins such as from scorpions or spiders . The toxins can be the synthesis and release of insecticidal and nematicidal delivered directly to the insect ' s gut or internal organs by toxic peptides in relatively large numbers at the site of injection or by inducing the insect to consume the toxin from activity , i . e . , the gut or other organs of the insect or nema its food , for example an insect feeding upon a transgenic tode. The synthesis in the host is facilitated by directed plant. These toxins have been known to have the ability to expression in regions of the host cell that enables proper inhibit the growth , impair the movement, or even kill an folding of the transgenic protein and enhances synthesis in insect when the toxin is delivered to the insect by spreading the host cell . the toxin to the locus inhabited by the insect or to the insect' s environment
Load more

Recommended publications
  • The Structure/Function of New Insecticidal Proteins and Regulatory Challenges for Commercialization
    This is an Open Access document downloaded from ORCA, Cardiff University's institutional repository: http://orca.cf.ac.uk/100278/ This is the author’s version of a work that was submitted to / accepted for publication. Citation for final published version: Moar, William, Berry, Colin and Narva, Kenneth 2017. The structure/function of new insecticidal proteins and regulatory challenges for commercialization. Journal of Invertebrate Pathology 142 , pp. 1-4. 10.1016/j.jip.2017.02.001 file Publishers page: https://doi.org/10.1016/j.jip.2017.02.001 <https://doi.org/10.1016/j.jip.2017.02.001> Please note: Changes made as a result of publishing processes such as copy-editing, formatting and page numbers may not be reflected in this version. For the definitive version of this publication, please refer to the published source. You are advised to consult the publisher’s version if you wish to cite this paper. This version is being made available in accordance with publisher policies. See http://orca.cf.ac.uk/policies.html for usage policies. Copyright and moral rights for publications made available in ORCA are retained by the copyright holders. The structure/function of new insecticidal proteins and regulatory challenges for commercialization William Moar, Colin Berry and Kenneth Narva Genetically modified crops produced by biotechnology methods have provided grower benefits since 1995 including improved protection of crop yield, reduced input costs, and a reduced reliance on chemical pesticides (Klumper and Qaim, 2014). These benefits have driven annual increases in worldwide adoption of GM crops, with the largest number of hectares being grown in the Americas (ISAAA 2014).
    [Show full text]
  • US Department of Agriculture
    Environmental Assessment for Dow/Pioneer Rootworm Resistant Corn APHIS’ Analysis and Response to Comments Received on Petition 03-353-01p and the EA. A total of two comments were submitted during the designated 60-day comment period by a private individual and a national trade association. The comment submitted by the trade association supported deregulation of the Cry34/35 Ab1 corn rootworm resistant corn (CRW). This comment stressed the importance of a different mechanism of control compared to the only CRW resistant corn product on the market while providing a new option for managing insect resistance. The commenter also mentioned that this product would provide a wider range of plant protection. The comment in opposition to deregulation of this product was submitted by a private citizen. This commenter expressed a general disapproval of genetically modified plants and suggested that this product should always be regulated. APHIS disagrees with this comment. The author fails to provide any information to support her assertion that this petition should be denied. The commenter also suggested that APHIS extend the comment period, but failed to provide a reason for the extension. Further, this commenter discussed pesticidal issues related to EPA’s role in the regulation of plant incorporated protectants. APHIS defers to EPA on issues related to EPA’s authority. - 2 - Environmental Assessment for Dow/Pioneer Rootworm Resistant Corn USDA/APHIS Decision on Dow AgroSciences and Pioneer Hi-Bred International Petition 03-353-01P Seeking a Determination of Nonregulated Status for Bt cry34/35Ab1 Insect Resistant Corn Line DAS-59122-7 Environmental Assessment TABLE OF CONTENTS I.
    [Show full text]
  • Bacillus Thuringiensis As a Specific, Safe, and Effective Tool for Insect Pest Control
    J. Microbiol. Biotechnol. (2007), 17(4), 547–559 Bacillus thuringiensis as a Specific, Safe, and Effective Tool for Insect Pest Control ROH, JONG YUL, JAE YOUNG CHOI, MING SHUN LI, BYUNG RAE JIN1, AND YEON HO JE* Department of Agricultural Biotechnology, College of Agriculture and Life Sciences, Seoul National University, Seoul 151-742, Korea 1College of Natural Resources and Life Science, Dong-A University, Busan 604-714, Korea Received: November 21, 2006 Accepted: January 2, 2007 Bacillus thuringiensis (Bt) was first described by Berliner The insecticidal bacterium Bt is a Gram-positive [10] when he isolated a Bacillus species from the Mediterranean bacterium that produces proteinaceous inclusions during flour moth, Anagasta kuehniella, and named it after the sporulation [53]. These inclusions can be distinguished as province Thuringia in Germany where the infected moth distinctively shaped crystals by phase-contrast microscopy. was found. Although this was the first description under The inclusions are composed of proteins known as crystal the name B. thuringiensis, it was not the first isolation. In proteins, Cry proteins, or δ-endotoxins, which are highly 1901, a Japanese biologist, Ishiwata Shigetane, discovered toxic to a wide variety of important agricultural and a previously undescribed bacterium as the causative health-related insect pests as well as other invertebrates. agent of a disease afflicting silkworms. Bt was originally Because of their high specificity and their safety for the considered a risk for silkworm rearing but it has become environment, crystal proteins are a valuable alternative the heart of microbial insect control. The earliest commercial to chemical pesticides for control of insect pests in production began in France in 1938, under the name agriculture and forestry and in the home.
    [Show full text]
  • The Pesticidal Cry6aa Toxin from Bacillus Thuringiensis Is Structurally
    Dementiev et al. BMC Biology (2016) 14:71 DOI 10.1186/s12915-016-0295-9 RESEARCH ARTICLE Open Access The pesticidal Cry6Aa toxin from Bacillus thuringiensis is structurally similar to HlyE- family alpha pore-forming toxins Alexey Dementiev1, Jason Board2, Anand Sitaram3, Timothy Hey4,7, Matthew S. Kelker4,10, Xiaoping Xu4, Yan Hu3, Cristian Vidal-Quist2,8, Vimbai Chikwana4, Samantha Griffin4, David McCaskill4, Nick X. Wang4, Shao-Ching Hung5, Michael K. Chan6, Marianne M. Lee6, Jessica Hughes2,9, Alice Wegener2, Raffi V. Aroian3, Kenneth E. Narva4 and Colin Berry2* Abstract Background: The Cry6 family of proteins from Bacillus thuringiensis represents a group of powerful toxins with great potential for use in the control of coleopteran insects and of nematode parasites of importance to agriculture. These proteins are unrelated to other insecticidal toxins at the level of their primary sequences and the structure and function of these proteins has been poorly studied to date. This has inhibited our understanding of these toxins and their mode of action, along with our ability to manipulate the proteins to alter their activity to our advantage. To increase our understanding of their mode of action and to facilitate further development of these proteins we have determined the structure of Cry6Aa in protoxin and trypsin-activated forms and demonstrated a pore-forming mechanism of action. Results: The two forms of the toxin were resolved to 2.7 Å and 2.0 Å respectively and showed very similar structures. Cry6Aa shows structural homology to a known class of pore-forming toxins including hemolysin E from Escherichia coli and two Bacillus cereus proteins: the hemolytic toxin HblB and the NheA component of the non- hemolytic toxin (pfam05791).
    [Show full text]
  • Molecular Mode of Action of Cry6aa1, a New Insecticidal Bacillus Thuringiensis Toxin
    i ii Université de Montréal Molecular mode of action of Cry6Aa1, a new insecticidal Bacillus thuringiensis toxin par Eva Fortea Verdejo Département de physiologie moléculaire et intégrative Faculté de médecine Mémoire présenté en vue de l’obtention du grade de Maîtrise en physiologie moléculaire, cellulaire et intégrative option physiologie et biophysique moléculaires Membres du jurée Lucie Parent, Réjean Couture et Jean-Louis Schwartz Août 2016 © Eva Fortea Verdejo, 2016 iii ABSTRACT Cry6Aa1 is a new toxin produced by Bacillus thuringiensis (Bt), which displays insecticidal activity against the Western corn rootworm (WCRW). The present work demonstrates that Cry6Aa1 is a pore-forming toxin (PFT) in planar lipid bilayers (PLBs). Contrary to other Bt toxins tested so far, pore formation by Cry6Aa1 does not require protease pretreatment and takes place at doses that are two to three orders of magnitude lower than those required for other Bt toxins under similar conditions. Pore formation by Cry6Aa1 is pH-dependent; the conductances of the pores range between 31 and 689 pS under symmetrical 150 mM KCl conditions; they are cationic and display a complex kinetic behaviour. The treatment of the toxin with midgut juice (Cry6Aa1 WCR1) does not change the biophysical properties of the pores. However, the treatment with trypsin (Cry6Aa1 TT) affects their conductance and selectivity at pH 5.5 (the WCRW gut physiological pH). The incorporation in PLBs of native membrane material from WCRW midgut affects the behaviour of the Cry6Aa1 pores. The molecular determinants of the mode of action of this new PFT appear therefore to differ from those reported before for other Bt toxins.
    [Show full text]
  • Technical Document for Bacillus Thuringiensis Cry34ab1 And
    BIOPESTICIDES REGISTRATION ACTION DOCUMENT Bacillus thuringiensis Cry34Ab1 and Cry35Ab1 Proteins and the Genetic Material Necessary for Their Production (PHP17662 T-DNA) in Event DAS-59122-7 Corn (OECD Unique Identifier: DAS-59122-7) PC Code: 006490 U.S. Environmental Protection Agency Office of Pesticide Programs Biopesticides and Pollution Prevention Division Bacillus thuringiensis Cry34/35Ab1 Corn Biopesticides Registration Action Document (BRAD) September 2010 Table of Contents I. OVERVIEW A. Background 4 B. Use Profile 7 C. Regulatory History 8 II. SCIENCE ASSESSMENT A. Product Characterization 14 B. Human Health Assessment 41 C. Environmental Assessment 66 D. Insect Resistance Management 117 E. Benefits 172 III. REGULATORY POSITION FOR EVENT DAS-59122-7 CORN A. Initial Registration (August 31, 2005) 193 B. 2010 Update 195 C. Period of Registration 197 APPENDIX A 199 2 Bacillus thuringiensis Cry34/35Ab1 Corn Biopesticides Registration Action Document (BRAD) September 2010 Bacillus thuringiensis Cry34Ab1 and Cry35Ab1 Proteins and the Genetic Material Necessary for Their Production (PHP17662 T-DNA) in Event DAS-59122-7 Corn Regulatory Action Team Product Characterization and Human Health Rebecca Edelstein, Ph.D. John Kough, Ph.D. Annabel Waggoner Chris Wozniak, Ph.D. Environmental Fate and Effects Joel Gagliardi, Ph.D. Hillary Hill Tessa Milofsky Robyn Rose Zigfridas Vaituzis, Ph.D. Annabel Waggoner Insect Resistance Management Jeannette Martinez Sharlene Matten, Ph.D. Tessa Milofsky Alan Reynolds Benefits Assessment Edward Brandt Sharlene Matten, Ph.D. Tessa Milofsky Registration Support Mike Mendelsohn Sheryl Reilly, Ph.D. Ann Sibold Biopesticides Registration Action Document Team Leaders Jeannine Kausch Mike Mendelsohn Office of General Counsel Angela Huskey, Esq. 3 Bacillus thuringiensis Cry34/35Ab1 Corn Biopesticides Registration Action Document (BRAD) September 2010 I.
    [Show full text]
  • Biopesticides Fact Sheet for Bacillus Thuringiensis Cry34ab1 And
    Bacillus thuringiensis Cry34Ab1 and Cry35Ab1 proteins and the genetic material necessary for their production (plasmid insert PHP 17662) in Event DAS-59122-7 corn (006490) Fact Sheet I. Description of the Plant-Incorporated Protectant o Pesticide Name: Bacillus thuringiensis Cry34Ab1 and Cry35Ab1 proteins and the genetic material necessary for their production (plasmid insert PHP 17662) in Event DAS-59122-7 corn o Date Registered: August 31, 2005 o Registration Numbers: 68467-5, 29964-4 o Trade and Other Names: Event DAS-59122-7 corn, Herculex Rootworm, Herculex RW o OPP Chemical Code: 006490 o Basic Manufacturers: Mycogen Seeds c/o Dow AgroSciences LLC 330 Zionsville Road, Indianapolis, IN 46268 Pioneer Hi-Bred International, A Dupont Company 7250 N.W. 62nd Ave., P.O. Box 552, Johnston, IA o Type of Pesticide: Plant-Incorporated Protectant o Uses: Field Corn o Target Pest(s): Corn Rootworm II. Background EPA has conditionally registered Mycogen Seeds c/o Dow AgroSciences LLC and Pioneer Hi-Bred International’s new active ingredient, Bacillus thuringiensis Cry34Ab1 and Cry35Ab1 proteins and the genetic material necessary for their production (plasmid insert PHP 17662) in Event DAS-59122- 7 corn. The Agency has determined that the use of this pesticide is in the public interest and that it will not cause any unreasonable adverse effects on the environment during the time of conditional registration. The new products are the second PIP to offer protection against corn rootworm (CRW), and they are expected to result in a further reduction of chemical insecticide use by growers. The reduced chemical pesticide use will benefit the environment directly and can mean less exposure to people who apply chemical pesticides to corn.
    [Show full text]
  • The European GMO-Free Citizens (De Gentechvrije Burgers) Country: the Netherlands Type: Others
    Maize MON89034x1507xMON88017x59122xDAS-40278-9 Organisation: The European GMO-free Citizens (De Gentechvrije Burgers) Country: The Netherlands Type: Others... a. Assessment: b. Food Safety Assessment: Toxicology Please refer to our previous complaints. International Immunopharmacology Volume 61, August 2018, Pages 185-196 Study of the allergenic potential of Bacillus thuringiensis Cry1Ac toxin following intra-gastric administration in a murine model of food-allergy Author links open overlay panel Karla I.Santos-Vigil et All https://doi.org/10.1016/j.intimp.2018.05.029 Allergenicity Research by Hoechst (Dr Arno Schulz) into the substrates of phosphinothricin acetyltransferase (PAT). ________________________________________ PAT, a GM product, occurs in herbicide (PPT)-resistant crops. Amsterdam, 7 November 1999 Two studies which gave rise to opposing conclusions, namely, 1. Charles J. Thompson, 1987: Characterization of the herbicide-resistance gene bar from Streptomyces hygroscopicus: 2. Dr Arno Schulz, 1993: L-Phosphinothricine N-Acetyl-transferase -Biochemical Characterization – a report which was incorporated into Wehrmann 1996 (Schulz is the co-author). The subject of the study is the characterisation of the enzyme phosphinotricin acetyltransferase (PAT) and more precisely the specificity of the substrates. The first study concerns the reaction of phosphinothricin with acetyl co-enzyme A under the influence of the PAT enzyme and compares it with a number of structural analogues of PPT phosphinothricin. One of the analogues was L-glutamate. The reaction products were identified using a mass spectrogram and the equilibrium constants (affinity) determined. In addition to phosphinothricin (PPT), a number of structural analogues were tested to determine if an acetylation reaction took place. L-glutamine acid was one of the substances studied.
    [Show full text]
  • Purification and Characterization of Recombinant Collagens/Gelatins from Transgenic Corn Seeds Cheng Zhang Iowa State University
    Iowa State University Capstones, Theses and Retrospective Theses and Dissertations Dissertations 2008 Purification and characterization of recombinant collagens/gelatins from transgenic corn seeds Cheng Zhang Iowa State University Follow this and additional works at: https://lib.dr.iastate.edu/rtd Part of the Agriculture Commons, Bioresource and Agricultural Engineering Commons, and the Chemical Engineering Commons Recommended Citation Zhang, Cheng, "Purification and characterization of recombinant collagens/gelatins from transgenic corn seeds" (2008). Retrospective Theses and Dissertations. 15737. https://lib.dr.iastate.edu/rtd/15737 This Dissertation is brought to you for free and open access by the Iowa State University Capstones, Theses and Dissertations at Iowa State University Digital Repository. It has been accepted for inclusion in Retrospective Theses and Dissertations by an authorized administrator of Iowa State University Digital Repository. For more information, please contact [email protected]. Purification and characterization of recombinant collagens/gelatins from transgenic corn seeds by Cheng Zhang A dissertation submitted to the graduate faculty in partial fulfillment of the requirements for the degree of DOCTOR OF PHILOSOPHY Major: Chemical Engineering Program of Study Committee: Charles E. Glatz, Major Professor Lawrence A. Johnson Patricia A. Murphy Balaji Narasimhan Peter J. Reilly Iowa State University Ames, Iowa 2008 Copyright © Cheng Zhang, 2008. All rights reserved. 3325543 3325543 2008 ii TABLE OF CONTENTS ABSTRACT iv CHAPTER 1. GENERAL INTRODUCTION 1 Motivation and Objectives 1 Dissertation Format 3 Literature Review 3 References 35 CHAPTER 2. PURIFICATION AND CHARACTERIZATION OF A 44 kDa RECOMBINANT COLLAGEN I alpha 1 FRAGMENT FROM CORN SEED 44 Abstract 44 Introduction 45 Materials and Methods 50 Results and Discussion 57 Conclusions 70 Acknowledgements 70 References 71 CHAPTER 3.
    [Show full text]
  • Bacillus Thuringiensis - Derived Insect Control Proteins
    Unclassified ENV/JM/MONO(2007)14 Organisation de Coopération et de Développement Economiques Organisation for Economic Co-operation and Development 26-Jul-2007 ___________________________________________________________________________________________ English - Or. English ENVIRONMENT DIRECTORATE JOINT MEETING OF THE CHEMICALS COMMITTEE AND Unclassified ENV/JM/MONO(2007)14 THE WORKING PARTY ON CHEMICALS, PESTICIDES AND BIOTECHNOLOGY Cancels & replaces the same document of 19 July 2007 SERIES ON HARMONISATION OF REGULATORY OVERSIGHT IN BIOTECHNOLOGY Number 42 CONSENSUS DOCUMENT ON SAFETY INFORMATION ON TRANSGENIC PLANTS EXPRESSING BACILLUS THURINGIENSIS - DERIVED INSECT CONTROL PROTEINS This document has been cancelled and replaced to correct mistakes in formatting due to technical problems. English - Or. English JT03230592 Document complet disponible sur OLIS dans son format d'origine Complete document available on OLIS in its original format ENV/JM/MONO(2007)14 Also published in the Series on Harmonisation of Regulatory Oversight in Biotechnology: No. 1, Commercialisation of Agricultural Products Derived through Modern Biotechnology: Survey Results (1995) No. 2, Analysis of Information Elements Used in the Assessment of Certain Products of Modern Biotechnology (1995) No. 3, Report of the OECD Workshop on the Commercialisation of Agricultural Products Derived through Modern Biotechnology (1995) No. 4, Industrial Products of Modern Biotechnology Intended for Release to the Environment: The Proceedings of the Fribourg Workshop (1996) No. 5, Consensus Document on General Information concerning the Biosafety of Crop Plants Made Virus Resistant through Coat Protein Gene-Mediated Protection (1996) No. 6, Consensus Document on Information Used in the Assessment of Environmental Applications Involving Pseudomonas (1997) No. 7, Consensus Document on the Biology of Brassica napus L. (Oilseed Rape) (1997) No.
    [Show full text]
  • Use of Cry1ab in Combination with Cry1be For
    (19) TZZ _¥¥__T (11) EP 2 513 318 B1 (12) EUROPEAN PATENT SPECIFICATION (45) Date of publication and mention (51) Int Cl.: of the grant of the patent: C12N 15/82 (2006.01) A01H 5/00 (2018.01) 24.01.2018 Bulletin 2018/04 A01H 5/10 (2018.01) A01N 63/02 (2006.01) A01N 65/00 (2009.01) (21) Application number: 10842620.6 (86) International application number: (22) Date of filing: 16.12.2010 PCT/US2010/060830 (87) International publication number: WO 2011/084631 (14.07.2011 Gazette 2011/28) (54) USE OF CRY1AB IN COMBINATION WITH CRY1BE FOR MANAGEMENT OF RESISTANT INSECTS VERWENDUNG VON CRY1AB IN KOMBINATION MIT CRY1BE ZUR BEKÄMPFUNG RESISTENTER INSEKTEN UTILISATION DE CRY1AB EN COMBINAISON AVEC CRY1BE POUR LA PRISE EN CHARGE D’INSECTES RÉSISTANTS (84) Designated Contracting States: • BURTON, Stephanie, L. AL AT BE BG CH CY CZ DE DK EE ES FI FR GB Indianapolis GR HR HU IE IS IT LI LT LU LV MC MK MT NL NO IN 46278 (US) PL PT RO RS SE SI SK SM TR Designated Extension States: (74) Representative: Zwicker, Jörk et al ME ZSP Patentanwälte PartG mbB Hansastraße 32 (30) Priority: 16.12.2009 US 284290 P 80686 München (DE) (43) Date of publication of application: (56) References cited: 24.10.2012 Bulletin 2012/43 US-A- 5 723 758 US-A- 5 990 390 US-A1- 2005 155 103 US-A1- 2008 311 096 (73) Proprietor: Dow AgroSciences, LLC Indianapolis, Indiana 46268 (US) • AHMAD ANWAAR ET AL: "Expression of synthetic cry1Ab and cry1Ac genes in Basmati (72) Inventors: rice (Oryza sativa L.) variety 370 via • MEADE, Thomas Agrobacterium-mediated transformation for the Zionsville control of the European corn borer (Ostrinia IN 46077 (US) nubilalis)", IN VITRO CELLULAR & • NARVA, Kenneth DEVELOPMENT BIOLOGY.
    [Show full text]
  • WO 2014/009175 Al 16 January 2014 (16.01.2014) P O PCT
    (12) INTERNATIONAL APPLICATION PUBLISHED UNDER THE PATENT COOPERATION TREATY (PCT) (19) World Intellectual Property Organization International Bureau (10) International Publication Number (43) International Publication Date WO 2014/009175 Al 16 January 2014 (16.01.2014) P O PCT (51) International Patent Classification: Maarten; 242 Ashton Glen Rd., Durham, NC 27703, A01N 37/40 (2006.01) A01N 25/30 (2006.01) 00000 (US). A01P 13/02 (2006.01) A O 57/20 (2006.01) (74) Common Representative: BASF SE; 67056 Ludwig- (21) International Application Number: shafen (DE). PCT/EP2013/063641 (81) Designated States (unless otherwise indicated, for every (22) International Filing Date: kind of national protection available): AE, AG, AL, AM, 28 June 2013 (28.06.2013) AO, AT, AU, AZ, BA, BB, BG, BH, BN, BR, BW, BY, BZ, CA, CH, CL, CN, CO, CR, CU, CZ, DE, DK, DM, (25) Filing Language: English DO, DZ, EC, EE, EG, ES, FI, GB, GD, GE, GH, GM, GT, (26) Publication Language: English HN, HR, HU, ID, IL, IN, IS, JP, KE, KG, KN, KP, KR, KZ, LA, LC, LK, LR, LS, LT, LU, LY, MA, MD, ME, (30) Priority Data: MG, MK, MN, MW, MX, MY, MZ, NA, NG, NI, NO, NZ, 61/669170 9 July 2012 (09.07.2012) US OM, PA, PE, PG, PH, PL, PT, QA, RO, RS, RU, RW, SC, 12176240.5 13 July 2012 (13.07.2012) EP SD, SE, SG, SK, SL, SM, ST, SV, SY, TH, TJ, TM, TN, 61/734383 7 December 2012 (07. 12.2012) US TR, TT, TZ, UA, UG, US, UZ, VC, VN, ZA, ZM, ZW.
    [Show full text]