Sympathetic Printed-Matter and Method of Producing the Same

Total Page:16

File Type:pdf, Size:1020Kb

Sympathetic Printed-Matter and Method of Producing the Same (19) TZZ¥_ Z_T (11) EP 3 168 270 A1 (12) EUROPEAN PATENT APPLICATION (43) Date of publication: (51) Int Cl.: 17.05.2017 Bulletin 2017/20 C09D 11/04 (2006.01) B41M 3/14 (2006.01) B41F 17/00 (2006.01) C09D 11/50 (2014.01) (21) Application number: 16185655.4 (22) Date of filing: 25.08.2016 (84) Designated Contracting States: (72) Inventors: AL AT BE BG CH CY CZ DE DK EE ES FI FR GB • LEE, Myoung Ku GR HR HU IE IS IT LI LT LU LV MC MK MT NL NO Gangwon-do (KR) PL PT RO RS SE SI SK SM TR • RYU, Jeong Yong Designated Extension States: Gangwon-do (KR) BA ME • KIM, Chang Geun Designated Validation States: Gangwon-do (KR) MA MD • LEE, Kwang Seob Gangwon-do (KR) (30) Priority: 13.11.2015 KR 20150159856 • LEE, Jae Hoon Gangwon-do (KR) (71) Applicants: • CHO, Han Je • Kwangwon National University Seoul (KR) Gangwon-do (KR) • KWON, Hyeok Jun • Daehan Paper Co., Ltd. Gyeonggi-do (KR) Chungcheongbuk-do (KR) • Taekyung Polymer Co., Ltd. (74) Representative: Wablat Lange Karthaus Gyeonggi-do (KR) Anwaltssozietät • Centre Technique de l’Industrie des Papiers, Potsdamer Chaussee 48 Cartons et Celluloses 14129 Berlin (DE) 38044 Grenoble Cedex 9 (FR) (54) SYMPATHETIC PRINTED-MATTER AND METHOD OF PRODUCING THE SAME (57) Using the sympathetic printed-matter according the sympathetic printed-matter has been read by any oth- to the present invention, a hidden content can be visual- er person can be easily determined. In the sympathetic ized just by wetting. Therefore, it is possible to remove printing method according to the present invention, a hy- necessities of the sympathetic ink and a special material drophobic substrate can be formed using an existing gas such as reagent or equipment for visualizing hidden con- grafting facility, and an ester hydrolase composition and tents. In addition, since the hidden contents disappear the reading confirmation portion can be formed using an by removing water from the sympathetic printed-matter, existing printing method. Therefore, a large amount of the sympathetic printed-matter can be used repeatedly. sympathetic printed-matters can be produced inexpen- Using the reading confirmation portion, whether or not sively and efficiently. EP 3 168 270 A1 Printed by Jouve, 75001 PARIS (FR) EP 3 168 270 A1 Description CROSS REFERENCES TO RELATED APPLICATIONS 5 [0001] The present invention contains subject matter related to Korean Patent Application No. 2015-0159856, filed in the Korean Patent Office on November 13, 2015, the entire contents of which are incorporated herein by reference. BACKGROUND OF THE INVENTION 10 Field of the Invention [0002] The present invention relates to a sympathetic printed-matter having a hydrophilic substrate portion formed on a hydrophobic substrate and a method of producing the same. 15 Description of Related Art [0003] As industries are developing, and competitions become violent, demands for convenient and reliable stega- nography increase. In particular, a sympathetic printing method using a sympathetic ink promotes new demands for anti-forgery techniques in the field of securities or exchange checks. Sympathetic printed-matters using a sympathetic 20 ink are advantageous in that a confidentiality status can be easily checked because whether or not a printed matter has been read by any other person can be easily confirmed. The term "sympathetic" means a phenomenon in which something is invisible on application or soon but can be visible later by developing the hidden parts. The sympathetic printed-matter is a printed matter produced using a sympathetic ink, on which a script written with a sympathetic ink can be visualized through heating or other methods such as a chemical reaction. The sympathetic ink may include a body fluid such as 25 blood, saliva, sweat, and urine, various foods or compounds containing acidic or basic properties such as vinegar, fruit juice, sodium bicarbonate, salt, sugar, rice, aspirin, Arabian gum, boric acid, starch, ammonia, magnesium sulfate (epsom salts), caustic silver, soap, glue, or adhesive. As a representative material of the sympathetic ink, lead acetate (Pb(CH3COO)2) is known in the art. The lead acetate has a colorless crystalline material obtained by dissolving lead monoxide (PbO) or tri-lead tetra-oxide (Pb 3O4) in acetic acid. A sympathetic ink is obtained by dissolving the lead acetate 30 in an alum solution. As a method of visualizing hidden contents written on a sympathetic printed-matter, there are known an optical method in which a hidden part is visualized by irradiating light using a special light source such as infrared or ultraviolet rays or irradiating such light at a particular angle, a mechanical method in which a hidden part is visualized by dispersing minute powder such as graphite and sweeping away the powder, and a physical chemical method in which a hidden part is visualized by exposing the sympathetic printed-matter in the hot air, fumes, or vapors of a chemical 35 agent or immersing it in a chemical agent. The sympathetic printed-matter using a sympathetic ink of the related art is based on an irreversible sympathetic phenomenon in which the printed part appears and does not disappear continuously thereafter. Even when it is reversible, it is difficult to know whether or not the hidden part of the sympathetic printed- matter has been already read by any other person. In addition, it is necessary to provide a separate reagent or tool for visualizing the hidden part on the sympathetic printed-matter. 40 [Citation List] [Patent Literatures] 45 [0004] [Patent Literature 1] Korean Patent No. 0173103 SUMMARY OF THE INVENTION [0005] In view of the aforementioned problems, the present invention provides a sympathetic printed-matter and a 50 method of producing the same, by which a hidden part can be visualized just by wetting, and the visualized part disappears by removing water, so that it can be reused repeatedly. In addition, the present invention provides a sympathetic printed- matter having a reading confirmation portion by which whether or not the hidden part has been read by any other person can be easily confirmed. [0006] According to an aspect of the present invention, there is provided a sympathetic printed-matter having a hy- 55 drophilic substrate portion formed on a hydrophobic substrate. [0007] According to an embodiment of the invention, the sympathetic printed-matter is formed without using a sym- pathetic ink. In the sympathetic printed-matter according to the present invention, visualization is performed based on a brightness difference between a wetted substrate and an unwetted substrate. Therefore, the sympathetic ink is not 2 EP 3 168 270 A1 necessary. [0008] According to another embodiment of the invention, the hydrophobic substrate is obtained by performing fatty- acid-chloride gas grafting for a substrate formed of a material containing a hydroxyl group (-OH) to hydrophobize the substrate. Preferably, the substrate formed of a material containing the hydroxyl group (-OH) is cellulose or polyvinyl 5 alcohol (PVA). More preferably, the substrate is a paper sheet or a paper board. Any substrate may be employed as long as it can be wetted by water. Considering print quality and use purposes, a paper sheet or a paper board having a high water absorption property is preferable. The fatty-acid-chloride grafting may be performed based on any gas grafting method known in the art (refer to Korean Patent Application Publication Nos. 10-2015-0077380 and 10-2015-0077379). 10 [0009] According to an implementation of the invention, the hydrophilic substrate portion is formed by partially printing an ester hydrolysis enzyme composition on the hydrophobic substrate. As a printing method of the enzyme composition, any method may be employed without a limitation as long as the enzyme composition can be printed on the hydrophobic substrate in a desired shape, and the enzyme composition can be sprayed uniformly with a constant thickness to uniformly generate the ester hydrolase reaction. 15 [0010] According to an implementation of the invention, the hydrophilic substrate portion additionally has a reading confirmation portion. The reading confirmation portion is used to irreversibly visualize whether or not a hidden part on the sympathetic printed-matter has been read by any other person. [0011] According to another aspect of the invention, there is provided a method of printing a sympathetic printed- matter having a hydrophilic substrate portion formed on a hydrophobic substrate, the method including: (a) forming a 20 hydrophobic substrate by performing gas grafting using fatty acid chloride; (b) partially printing an ester hydrolase composition of 0.3 to 0.7 g/m 2 on the hydrophobic substrate and generate a reaction for 20 to 40 minutes under a room temperature to form a hydrophilic substrate portion; (c) washing and drying the hydrophobic substrate having the hy- drophilic substrate portion; and (d) printing a reading confirmation portion on the hydrophilic substrate portion. [0012] Other objects and technical characteristics of the present invention will become apparent by reading the following 25 description, claims, and drawings. BRIEF DESCRIPTION OF THE DRAWINGS [0013] The foregoing and additional features and characteristics of this disclosure will become more apparent from 30 the following detailed description considered with reference to the accompanying drawings, wherein: FIG. 1 illustrates a reversible sympathetic phenomenon of a sympathetic printed-matter. DETAILED DESCRIPTION OF THE INVENTION 35 [0014] The present invention provides a sympathetic printed-matter in which a hydrophobic substrate portion and a hydrophilic substrate portion are formed distinguishably, hidden contents are visualized by wetting, the hidden contents disappear by drying, and a reading confirmation portion is formed to allow a user to confirm whether or not the hidden contents have been read by any other person. 40 <Sympathetic Printed-Matter> [0015] The term "sympathetic printed-matter" means a printed matter or sheet on which contents such as scripts, symbols, or pictures are invisible in ordinary times, and they are visualized when a particular condition is satisfied.
Recommended publications
  • METACYC ID Description A0AR23 GO:0004842 (Ubiquitin-Protein Ligase
    Electronic Supplementary Material (ESI) for Integrative Biology This journal is © The Royal Society of Chemistry 2012 Heat Stress Responsive Zostera marina Genes, Southern Population (α=0.
    [Show full text]
  • Peroxidase Activity As an Indicator of the Iron Deficiency in Banana
    IndianJ Plant Physiol., Vol. 5, No.4, (N.S.) pp. 389-391 (Oct.-Dec., 2000) SHORT COMMUNICATION PEROXIDASE ACTIVITY AS AN INDICATOR OF THE IRON DEFICIENCY IN BANANA K. BALAKRISHNAN Department ofCrop Physiology, Horticultural College and Research Institute, Periyakulam - 625 604 Received on 30 Sept., 1998, Revised on 30 Nov., 2000 Effect oflime induced iron chlorosis on enzyme activities was studied in Banana cv. Rasthali. Iron content decreased progressively as the intensity of chlorosis increased. Iron content had positive correlation with catalase, peroxidase, acid phosphatase, polyphenol oxidase and nitrate reductase. Among the enzymes, the activityofperoxidasehad highest positivesignificant(r=997**) associationwith Fecontent. Hence, peroxidase activity could serve as a diagnostic tool to indentify the Fe deficiency/Fe status in Banana. Key words: Banana, chlorosis, iron, peroxidase Among the micrountrients, Fe deficiency is the most ofgreenness in sixmonths old crop. This leafwas used for widespread in ourcountry(Takkar, 1996). Iron deficiency all the physiological analysis viz chlorophyll (Yoshida et is very common in calcareous soils and hence termed as al., 1976) chlorophyllase (Almela et al., 1990), catalase, lime induced iron chlorosis. In a normal green plant 60% peroxidase and polyphenol oxidase (Kar and Mishra, ofall leafiron is present in the chlorophyIl and hence any 1976), acid phosphatase (Parida and Mishra, 1980) and reduction in Fe contentcauses chlorosis (Chen and Barak, nitrate reductase (Klepperetal., 1973). The Fe content of 1982). Iron deficiency in plant not only causes chlorosis the plant sample was estimated using atomic absorption because of its involvement in chlorophyll synthesis, but spectrophotometry. Data were subjected to simple also reduces the activity ofcertain enzymes viz., catalase correlation co-efficient.
    [Show full text]
  • Tepzz¥5Z5 8 a T
    (19) TZZ¥Z___T (11) EP 3 505 181 A1 (12) EUROPEAN PATENT APPLICATION (43) Date of publication: (51) Int Cl.: 03.07.2019 Bulletin 2019/27 A61K 38/46 (2006.01) C12N 9/16 (2006.01) (21) Application number: 18248241.4 (22) Date of filing: 28.12.2018 (84) Designated Contracting States: (72) Inventors: AL AT BE BG CH CY CZ DE DK EE ES FI FR GB • DICKSON, Patricia GR HR HU IE IS IT LI LT LU LV MC MK MT NL NO Torrance, CA California 90502 (US) PL PT RO RS SE SI SK SM TR • CHOU, Tsui-Fen Designated Extension States: Torrance, CA California 90502 (US) BA ME • EKINS, Sean Designated Validation States: Brooklyn, NY New York 11215 (US) KH MA MD TN • KAN, Shih-Hsin Torrance, CA California 90502 (US) (30) Priority: 28.12.2017 US 201762611472 P • LE, Steven 05.04.2018 US 201815946505 Torrance, CA California 90502 (US) • MOEN, Derek R. (71) Applicants: Torrance, CA California 90502 (US) • Los Angeles Biomedical Research Institute at Harbor-UCLA Medical Center (74) Representative: J A Kemp Torrance, CA 90502 (US) 14 South Square • Phoenix Nest Inc. Gray’s Inn Brooklyn NY 11215 (US) London WC1R 5JJ (GB) (54) PREPARATION OF ENZYME REPLACEMENT THERAPY FOR MUCOPOLYSACCHARIDOSIS IIID (57) The present disclosure relates to compositions for use in a method of treating Sanfilippo syndrome (also known as Sanfilippo disease type D, Sanfilippo D, mu- copolysaccharidosis type IIID, MPS IIID). The method can entail injecting to the spinal fluid of a MPS IIID patient an effective amount of a composition comprising a re- combinant human acetylglucosamine-6-sulfatase (GNS) protein comprising the amino acid sequence of SEQ ID NO: 1 or an amino acid sequence having at least 90% sequence identity to SEQ ID NO: 1 and having the en- zymatic activity of the human GNS protein.
    [Show full text]
  • Phospholipases, Nucleic Acids Encoding Them and Methods for Making and Using Them
    (19) TZZ¥_Z_ _T (11) EP 3 190 182 A1 (12) EUROPEAN PATENT APPLICATION (43) Date of publication: (51) Int Cl.: 12.07.2017 Bulletin 2017/28 C12N 9/20 (2006.01) C12N 1/20 (2006.01) C12N 15/00 (2006.01) C07H 21/04 (2006.01) (21) Application number: 16184319.8 (22) Date of filing: 08.03.2005 (84) Designated Contracting States: • FIELDING, Roderick AT BE BG CH CY CZ DE DK EE ES FI FR GB GR San Diego, CA 92109 (US) HU IE IS IT LI LT LU MC NL PL PT RO SE SI SK TR • BROWN, Robert C. San Diego, CA 92130 (US) (30) Priority: 08.03.2004 US 796907 • VASAVADA, Amit Poway, CA 92064 (US) (62) Document number(s) of the earlier application(s) in • TAN, Xuqiu accordance with Art. 76 EPC: San Diego, CA 92130 (US) 05727242.9 / 1 748 954 • BADILLO, Adrian Poway, CA 92064 (US) (27) Previously filed application: • VAN HOEK, Wilhelmus P. 08.03.2005 PCT/US2005/007908 San Diego, CA 92126 (US) • JANSSEN, Giselle (71) Applicant: DSM IP Assets B.V. San Diego, CA 92121 (US) 6411 TE Heerlen (NL) • ISAAC, Charles Carlsbad, CA 92008 (US) (72) Inventors: • BURK, Mark J. • GRAMATIKOVA, Svetlana San Diego, CA 92130 (US) San Diego, CA 92122 (US) • HAZLEWOOD, Geoff (74) Representative: Cazemier, Anne Engeline et al San Diego, CA 92130 (US) DSM Intellectual Property •LAM,David P.O. Box 4 Encinitas, CA 92024 (US) 6100 AA Echt (NL) • BARTON, Nelson R. San Diego, CA 92131 (US) Remarks: • STURGIS, Blake G. •A request for correction of the description has been Solana Beach, CA 92075 (US) filed pursuant to Rule 139 EPC.
    [Show full text]
  • Legionella Genus Genome Provide Multiple, Independent Combinations for Replication in Human Cells
    Supplemental Material More than 18,000 effectors in the Legionella genus genome provide multiple, independent combinations for replication in human cells Laura Gomez-Valero1,2, Christophe Rusniok1,2, Danielle Carson3, Sonia Mondino1,2, Ana Elena Pérez-Cobas1,2, Monica Rolando1,2, Shivani Pasricha4, Sandra Reuter5+, Jasmin Demirtas1,2, Johannes Crumbach1,2, Stephane Descorps-Declere6, Elizabeth L. Hartland4,7,8, Sophie Jarraud9, Gordon Dougan5, Gunnar N. Schroeder3,10, Gad Frankel3, and Carmen Buchrieser1,2,* Table S1: Legionella strains analyzed in the present study Table S2: Type IV secretion systems predicted in the genomes analyzed Table S3: Eukaryotic like domains identified in the Legionella proteins analyzed Table S4: Small GTPases domains detected in the genus Legionella as defined in the CDD ncbi domain database Table S5: Eukaryotic like proteins detected in the Legionella genomes analyzed in this study Table S6: Aminoacid identity of the Dot/Icm components in Legionella species with respect to orthologous proteins in L. pneumophila Paris Table S7: Distribution of seventeen highly conserved Dot/Icm secreted substrates Table S8: Comparison of the effector reperotoire among strains of the same Legionella species Table S9. Number of Dot/Icm secreted proteins predicted in each strain analyzed Table S10: Replication capacity of the different Legionella species analyzed in this study and collection of literature data on Legionella replication Table S11: Orthologous table for all genes of the 80 analyzed strains based on PanOCT. The orthologoss where defined with the program PanOCT using the parameters previously indicated in material and methods.) Figure S1: Distribution of the genes predicted to encode for the biosynthesis of flagella among all Legionella species.
    [Show full text]
  • Tannin Degradation by Phytopathogen's Tannase: a Plant's
    Biocatalysis and Agricultural Biotechnology 21 (2019) 101342 Contents lists available at ScienceDirect Biocatalysis and Agricultural Biotechnology journal homepage: http://www.elsevier.com/locate/bab Tannin degradation by phytopathogen’s tannase: A Plant’s defense perspective Kanti Prakash Sharma Department of Biosciences, Mody University of Science and Technology, Lakshmangarh, Sikar, Rajasthan, 332311, India ARTICLE INFO ABSTRACT Keywords: Tannins are plant secondary metabolites and characterized as plant defensive molecules. They impose a barrier Tannin against phytopathogens invasion in plants and thus oppose diseases occurrence in them. Tannase is an enzyme Tannase known for its ability to degrade plant tannins. Important plant pathogens also possess tannase coding sequence in Plant defense their genome. Researches on tannase are till date focused on its applications in animal nutrition, in bioreme­ Pathogen diation and in food industries etc. The information about tannase role with respect to pathogen’s virulence is Virulence very scanty or almost nil in scientific literature. The presence of tannase in pathogen’s genome is an adaptive feature which may be a part of its strategy to overcome the negative effects of plants tannins. The present review summarizes important aspects of tannase and its possible role in disease causing ability of pathogens in plants. 1. Introduction hydrolyzable tannins (Zhang et al., 2001). In complex tannins, a cate­ chin or epicatechin unit is bound glycosidically to a gallotannin or an Tannins are universally present in plants and represent the fourth ellagitannin unit to yield catechin or epicatechin and gallic acid or most abundant group of secondary metabolites after cellulose, hemi­ ellagic acid upon hydrolysis.
    [Show full text]
  • Comparative Study of Idursulfase Beta and Idursulfase in Vitro and in Vivo
    Journal of Human Genetics (2017) 62, 167–174 OPEN Official journal of the Japan Society of Human Genetics www.nature.com/jhg ORIGINAL ARTICLE Comparative study of idursulfase beta and idursulfase in vitro and in vivo Chihwa Kim1, Jinwook Seo2, Yokyung Chung2, Hyi-Jeong Ji3, Jaehyeon Lee2, Jongmun Sohn2, Byoungju Lee2 and Eui-cheol Jo1 Hunter syndrome is an X-linked lysosomal storage disease caused by a deficiency in the enzyme iduronate-2-sulfatase (IDS), leading to the accumulation of glycosaminoglycans (GAGs). Two recombinant enzymes, idursulfase and idursulfase beta are currently available for enzyme replacement therapy for Hunter syndrome. These two enzymes exhibited some differences in various clinical parameters in a recent clinical trial. Regarding the similarities and differences of these enzymes, previous research has characterized their biochemical and physicochemical properties. We compared the in vitro and in vivo efficacy of the two enzymes on patient fibroblasts and mouse model. Two enzymes were taken up into the cell and degraded GAGs accumulated in fibroblasts. In vivo studies of two enzymes revealed similar organ distribution and decreased urinary GAGs excretion. Especially, idursulfase beta exhibited enhanced in vitro efficacy for the lower concentration of treatment, in vivo efficacy in the degradation of tissue GAGs and improvement of bones, and revealed lower anti-drug antibody formation. A biochemical analysis showed that both enzymes show largely a similar glycosylation pattern, but the several peaks were different and quantity of aggregates of idursulfase beta was lower. Journal of Human Genetics (2017) 62, 167–174; doi:10.1038/jhg.2016.133; published online 10 November 2016 INTRODUCTION secreted protein and contains eight N-linked glycosylation sites at Mucopolysaccharidosis II (MPS II, Hunter syndrome; OMIM 309900) positions 31, 115, 144, 246, 280, 325, 513 and 537.
    [Show full text]
  • Sanfilippo Disease Type D: Deficiency of N-Acetylglucosamine-6- Sulfate Sulfatase Required for Heparan Sulfate Degradation
    Proc. Nat!. Acad. Sci. USA Vol. 77, No. 11, pp. 6822-6826, November 1980 Medical Sciences Sanfilippo disease type D: Deficiency of N-acetylglucosamine-6- sulfate sulfatase required for heparan sulfate degradation (mucopolysaccharidosis/keratan sulfate/lysosomes) HANS KRESSE, EDUARD PASCHKE, KURT VON FIGURA, WALTER GILBERG, AND WALBURGA FUCHS Institute of Physiological Chemistry, Waldeyerstrasse 15, D-4400 Mfinster, Federal Republic of Germany Communicated by Elizabeth F. Neufeld, July 10, 1980 ABSTRACT Skin fibroblasts from two patients who had lippo syndromes and excreted excessive amounts of heparan symptoms of the Sanfilippo syndrome (mucopolysaccharidosis sulfate and keratan sulfate in the urine. His fibroblasts were III) accumulated excessive amounts of hean sulfate and were unable to desulfate N-acetylglucosamine-6-sulfate and the unable to release sulfate from N-acety lucosamine)--sulfate linkages in heparan sulfate-derived oligosaccharides. Keratan corresponding sugar alcohol (17, 18). It was therefore suggested sulfate-derived oligosaccharides bearing the same residue at that N-acetylglucosamine-6-sulfate sulfatase is involved in the the nonreducing end and p-nitrophenyl6sulfo-2-acetamido- catabolism of both types of macromolecules. 2-deoxy-D-ucopyranoside were degraded normally. Kinetic In this paper, we describe a new disease, tentatively desig- differences between the sulfatase activities of normal fibro- nated Sanfilippo disease type D, that is characterized by the blasts were found. These observations suggest that N-acetyl- excessive excretion glucosamine4-6sulfate sulfatase activities degrading heparan clinical features of the Sanfilippo syndrome, sulfate and keratan sulfate, respectively, can be distinguished. of heparan sulfate, and the inability to release inorganic sulfate It is the activity directed toward heparan sulfate that is deficient from N-acetylglucosamine-6-sulfate residues of heparan sul- in these patients; we propose that this deficiency causes Sanfi- fate-derived oligosaccharides.
    [Show full text]
  • Letters to Nature
    letters to nature Received 7 July; accepted 21 September 1998. 26. Tronrud, D. E. Conjugate-direction minimization: an improved method for the re®nement of macromolecules. Acta Crystallogr. A 48, 912±916 (1992). 1. Dalbey, R. E., Lively, M. O., Bron, S. & van Dijl, J. M. The chemistry and enzymology of the type 1 27. Wolfe, P. B., Wickner, W. & Goodman, J. M. Sequence of the leader peptidase gene of Escherichia coli signal peptidases. Protein Sci. 6, 1129±1138 (1997). and the orientation of leader peptidase in the bacterial envelope. J. Biol. Chem. 258, 12073±12080 2. Kuo, D. W. et al. Escherichia coli leader peptidase: production of an active form lacking a requirement (1983). for detergent and development of peptide substrates. Arch. Biochem. Biophys. 303, 274±280 (1993). 28. Kraulis, P.G. Molscript: a program to produce both detailed and schematic plots of protein structures. 3. Tschantz, W. R. et al. Characterization of a soluble, catalytically active form of Escherichia coli leader J. Appl. Crystallogr. 24, 946±950 (1991). peptidase: requirement of detergent or phospholipid for optimal activity. Biochemistry 34, 3935±3941 29. Nicholls, A., Sharp, K. A. & Honig, B. Protein folding and association: insights from the interfacial and (1995). the thermodynamic properties of hydrocarbons. Proteins Struct. Funct. Genet. 11, 281±296 (1991). 4. Allsop, A. E. et al.inAnti-Infectives, Recent Advances in Chemistry and Structure-Activity Relationships 30. Meritt, E. A. & Bacon, D. J. Raster3D: photorealistic molecular graphics. Methods Enzymol. 277, 505± (eds Bently, P. H. & O'Hanlon, P. J.) 61±72 (R. Soc. Chem., Cambridge, 1997).
    [Show full text]
  • BARNES-DISSERTATION-2016.Pdf (1.557Mb)
    ABSORPTION AND METABOLISM OF MANGO (MANGIFERA INDICA L.) GALLIC ACID AND GALLOYL GLYCOSIDES A Dissertation by RYAN CRISPEN BARNES Submitted to the Office of Graduate and Professional Studies of Texas A&M University in partial fulfillment of the requirements for the degree of DOCTOR OF PHILOSOPHY Chair of Committee, Stephen Talcott Co-Chair of Committee, Susanne Talcott Committee Members, Nancy Turner Arul Jayaraman Head of Department, Boon Chew December 2016 Major Subject: Food Science and Technology Copyright 2016 Ryan Barnes ABSTRACT The composition, absorption, metabolism, and excretion of gallic acid, monogalloyl glucose, and gallotannins in mango (Mangifera indica L.) pulp were investigated. Each galloyl derivative was hypothesized to have a different rate of absorption, and their concentrations were compared in the pulp of five mango varieties. The cultivar Ataulfo was found to have the highest concentration of monogalloyl glucose and gallotannins while the cultivar Kent had the lowest. Enzymatic hydrolysis of gallotannins with tannase led to the characterization of six digalloyl glucoses and five trigalloyl glucoses that have the potential to be formed in the colon following gallotannin consumption. The bioaccessibility of galloyl derivatives was evaluated in both homogenized mango pulp and 0.65 mm3 cubes following in vitro digestion conditions. Monogalloyl glucose was found to be bioaccessible in both homogenized and cubed mango pulp. However, cubed mango pulp had a significantly higher amount of gallotannins still bound to the fruit following digestion. Gallic acid bioaccessibility significantly increased following digestion in both homogenized and cubed mango pulp, likely from hydrolysis of gallotannins. Additionally, for the first time, the absorption of monogalloyl glucose and gallic acid was investigated in both Caco-2 monolayer transport models and a porcine pharmacokinetic model with no significant differences found in their absorption or ability to produce phase II metabolites.
    [Show full text]
  • Nummer 18/17 03 Mei 2017 Nummer 18/17 2 03 Mei 2017
    Nummer 18/17 03 mei 2017 Nummer 18/17 2 03 mei 2017 Inleiding Introduction Hoofdblad Patent Bulletin Het Blad de Industriële Eigendom verschijnt The Patent Bulletin appears on the 3rd working op de derde werkdag van een week. Indien day of each week. If the Netherlands Patent Office Octrooicentrum Nederland op deze dag is is closed to the public on the above mentioned gesloten, wordt de verschijningsdag van het blad day, the date of issue of the Bulletin is the first verschoven naar de eerstvolgende werkdag, working day thereafter, on which the Office is waarop Octrooicentrum Nederland is geopend. Het open. Each issue of the Bulletin consists of 14 blad verschijnt alleen in elektronische vorm. Elk headings. nummer van het blad bestaat uit 14 rubrieken. Bijblad Official Journal Verschijnt vier keer per jaar (januari, april, juli, Appears four times a year (January, April, July, oktober) in elektronische vorm via www.rvo.nl/ October) in electronic form on the www.rvo.nl/ octrooien. Het Bijblad bevat officiële mededelingen octrooien. The Official Journal contains en andere wetenswaardigheden waarmee announcements and other things worth knowing Octrooicentrum Nederland en zijn klanten te for the benefit of the Netherlands Patent Office and maken hebben. its customers. Abonnementsprijzen per (kalender)jaar: Subscription rates per calendar year: Hoofdblad en Bijblad: verschijnt gratis Patent Bulletin and Official Journal: free of in elektronische vorm op de website van charge in electronic form on the website of the Octrooicentrum Nederland.
    [Show full text]
  • Ethylene Induces De Novo Synthesis of Chlorophyllase, a Chlorophyll
    Proc. Natl. Acad. Sci. USA Vol. 90, pp. 9441-9445, October 1993 Plant Biology Ethylene induces de novo synthesis of chlorophyllase, a chlorophyll degrading enzyme, in Citrus fruit peel (ripening/senescence/gibbereilin A3/N6-benzyladenine) TOVA TREBITSH, ELIEZER E. GOLDSCHMIDT, AND JOSEPH Riov The Kennedy-Leigh Centre for Horticultural Research, Faculty of Agriculture, The Hebrew University of Jerusalem, Rehovot 76100, Israel Communicated by Kenneth V. Thimann, July 15, 1993 ABSTRACT Chlorophyllase (Chlase; EC 3.1.1.14) was to induce a severalfold increase in Chlase activity (8-10). It extracted from plastid fractions of ethylene-treated orange is not known, however, whether this increase involves de fruit peel and purified 400-fold to homogeneity by gel iftration, novo synthesis of the enzyme protein or activation of a hydrophobic chromatography, and preparative SDS/PAGE of constitutive enzyme. Gibberellin A3 (GA) and N6-benzylad- nonheated protein. SDS/PAGE of nonheated purified enzyme enine (BA) delay the senescent pigment changes and oppose indicated that Chlase activity is associated with a single protein the ethylene-induced loss of Chl (6, 7, 11), but their effect on band migrating at an apparent molecular mass of 25 kDa Chlase activity has not yet been determined. Thus, little is whereas the heated purified enzyme had a molecular mass of35 known about the hormonal and molecular regulation of the kDa. The N-terminal sequence of the purified protein was Chlase enzyme system. determined. The purified enzyme was used as an immunogen While attempting to study the overall regulation of Chlase, for raising antibodies in rabbits. The antiserum was highly we found it essential to adopt an immunological approach.
    [Show full text]