United States Patent 119] [11] Patent Number: 4,576,817 Montgomery Et Al

Total Page:16

File Type:pdf, Size:1020Kb

United States Patent 119] [11] Patent Number: 4,576,817 Montgomery Et Al United States Patent 119] [11] Patent Number: 4,576,817 Montgomery et al. [45] Date of Patent: Mar. 18, 1986 [54] ENZYMATIC BANDAGES AND PADS 4,226,232 lO/l980 Spence .............................. .. 128/156 Inventors: Robert E. Montgomery, Paci?c 4,269,822 5/1981 14111666141. ......... .. .. 424/94x [75] 4,379,141 4/1983 Hasegawa 61 al. ............. .. 424/94 Palisades; Michael A. Pellico, Los 4,476,108 lO/l984 108851616441. ........ .. 424/13ox Angeles, both of Calif. 4,486,408 12/1984 Kiel ......................... .. 424/94 [73] Assignee: Laclede Professional Products, Inc., 4,537,764 8/1985 Pellico et al. ................... .. 424/94 X Gardena, Calif. FOREIGN PATENT DOCUMENTS [21] Appl. No.: 618,071 2488797 2/1982 France ................................ .. 424/94 [22] Filed: Jun. 7, 1984 Primary Examiner—Helen M. McCarthy Attorney, Agent, or Firm—Donald Diamond [51] Int. Cl.‘ . ......... .. A61K 37/48 [52] U.S. Cl. .......... .. ........................ .. 424/94; 128/127; [57] ABSTRACT 128/156; 424/ 130; 435/25; 604/375; 604/904 [58] Field of Search ............. .. 604/289, 369, 375, 904; Enzymatic absorbent materials such as bandages and 424/14, 94, 130; 128/127, 130, 156; 435/25 pads, for body contact applications, contain serum activated oxidoreductase enzyme for producing hydro [56] References Cited gen peroxide upon contact of the enzymatic materials U.S. PATENT DOCUMENTS with serum. An illustrative serum-activated oxidore 4,031,202 6/1977 Laughlin et al. ............. .. 128/130 X ductase enzyme is glucose oxidase with the correspond 4,122,158 10/1978 Schmitt ........................... .. 424/94 X ing substrate in serum being glucose. 4,150,113 4/1979 Hoogendoorn et al. ........... .. 424/50 4,178,362 12/1979 Hoogendoorn et al. ....... .. 424/94 X 20 Claims, No Drawings 4,576,817 1 2 It would, of course, be advantageous to provide ab ENZYMATIC BANDAGES AND PADS sorbent materials in the form of bandages, pads, strings and the like that would inhibit bacterial growth in body BACKGROUND OF THE INVENTION ?uids which are absorbed by or otherwise associated This invention relates to absorbent materials adapted with such absorbent materials or structures. for use in body contact applications and, more particu It is disclosed in the prior art that polymeric wound larly, to enzymatic absorbent materials such as ban dressings for burns may include antibacterial agents, dages and pads that produce a bacteriostatic effect upon antibiotics, antifungal agents, proteolytic enzymes as contact with body ?uids such as serum. well as local anesthetics, hormonal compounds and Absorbent materials in the form of bandages and pads lubricating and barrier chemicals. See, for example, have long been employed in body contact applications U.S. Pat. No. 4,122,158 (Schmitt, 1978) and U.S. Pat. where coverage and protection of a wound and absorp No. 4,226,232 (Spence, 1980). tion of its ?uids are desirable. Bandaging can serve to It is also disclosed in the prior art that enzymatic physically protect an open wound from the surrounding agents can be incorporated into oral products such as environment, which is often replete with harmful bac toothpaste and chewing gum for producing hydrogen teria, and to absorb ?uid materials such as pus, blood peroxide during oral use. and serum to thereby promote the healing of the U.S. Pat. No. 4,150,113 (Hoogendoom et al., 1979) wound. Accordingly, bandages are constructed of and U.S. Pat. No. 4,178,362 (Hoogendoom et al., 1979) strong, yet absorbent, materials such that retention of disclose, respectively, an enzymatic toothpaste and an extraneous ?uids can be accomplished without a con enzymatic chewable dentifrice containing glucose oxi commitant loss of strength. dase which acts on glucose present in saliva and tooth Absorbent materials such as woven ?bers, porous plaque to produce hydrogen peroxide. The patentees foam pads, absorbent membranes and solvent-based note that oral bacteria, through enzymes systems having porous elastomers have been utilized in the manufacture SH-GROUPS, effect glycolysis of food products con of bandages and pads. A wide of variety of raw materi taining sugars and point out that lactoperoxidase, which als have been employed in an attempt to obtain physi is present in saliva, provides the means for transferring cally occlusive structures that retain their strength oxygen from hydrogen peroxide to the oral bacteria when soaked with ?uid from an open or weeping resulting in the oxidation of the SH-containing enzymes wound or other body ?uid source. Materials such as into inactive disul?de enzymes. It is further disclosed cellulose and its derivatives (cellulosics), polyester, 30 that the dentifrice may be formulated with potassium nylon, polyacrylamide, collagen, polyurethane and pol thiocyanate. yvinyl alcohol have been fabricated into structures such U.S. Pat. No. 4,269,822 (Pellico et al., 1981) discloses as woven ?bers, foam pads, porous membranes, elasto an antiseptic dentifrice containing an oxidizable amino mers and multi-layered combinations of the aforemen acid substrate and an oxidoreductase enzyme speci?c to tioned structures. Regardless of the material used, all such substrate for producing hydrogen peroxide and bandages and pads employed in the protection of open ammonia upon oral application of the dentifrice, with wounds must satisfy the requirement of good absor pre-application stability being maintained by limiting bency in order to be effective. the quantity of any water present in the dentifrice. An absorbent material in contact with an open or SUMMARY OF THE INVENTION weeping wound will retain a substantial amount of In accordance with one aspect of this invention, there blood, blood serum, pus and a variety of wound exu is provided enzymatic absorbent material for body dates. Bandages are often constructed in such a way that moisture retained by the absorbent material in contact application containing, per gram of material, from about 1.0 to about 1,000 International Units of contact with the wound will transpire through the side 45 serum-activated oxidoreductase enzyme for producing of the bandage opposite to that of the source of the hydrogen peroxide upon contact of said material with ?uids, i.e., the open wound. Although structures such as serum. these tend to decrease the amount of moisture retained In accordance with a second aspect of this invention, by the absorbent material, other exudates such as white there is provided enzymatic absorbent ?ber for conver blood cells, bacteria, eletrolytes, and red blood cells are sion into enzymatic absorbent material that is adapted retained. These exudates accumulate as a function of the for body contact application, wherein the ?ber con amount of time an absorbent material is in contact with tains, per gram of ?ber, from about 1.0 to about 1,000 an open or weeping wound. International Units of serum-activated oxidoreductase As a result of the retention of such a wide variety of enzyme for producing hydrogen peroxide upon contact biological substances, a moist absorbent structure can with serum. become an effective breeding ground for potentially harmful bacteria. Such an absorbent structure in contact DETAILED DESCRIPTION with body ?uid of the type mentioned above can be The enzymatic absorbent materials of this invention characterized as a culture support medium that can give comprise ?uid absorbent structures that incorporate rise to a large number of potentially harmful bacterial serum-activated oxidoreductase enzyme for producing colonies in a relatively small volume. Since the accumu hydrogen peroxide upon contact with serum. Fluid lated bacteria and their ‘waste products remain in absorbent structures, in the form of bandages, pads, contact with the open or weeping wound, they can strips and the like, can be prepared from precursors and leach out of the absorbent structure and back to the by processes well-known in the art to provide appropri body. In this connection, symptoms classi?able as toxic 65 ate designs and con?gurations that are adapted for par shock syndrome have been associated with the use of ticular body contact applications. Structural precursors certain types of feminine hygiene tampons, i.e., inter such as woven ?bers, porous foam pads, absorbent nally disposed feminine hygiene absorbent pads. membranes and solvent-based porous elastomers can be 4,576,817 3 4 utilized in the manufacture of the ?uid absorbent struc Oxygen-accepting anions in serum include thiocya tures. Gauze bandaging alone or secured to adhesive nate, chloride and iodide ions which, in the presence of strip and feminine hygiene absorbent pads and tampons, hydrogen peroxide and peroxidase, are oxidized to as well as other externally and internally utilizable body hypothiocyante, hypochlorite and hypoiodite, respec contact devices having high absorbency characteristics, tively. can be advantageously utilized in the practice of this The enzymatic absorbent material described herein invention. may be augmented by additionally incorporating into The enzymatic absorbent material of this invention, the material supplementary ingredients as, for example, which incorporates oxidoreductase enzyme, is adapted (a) oxidizable substrate speci?c to the oxidoreductase to be used in body contact applications that encounter enzyme utilized in the material, and (b) oxidizable salt body ?uids. These ?uids, including blood and tissue such as the thiocyanate, chloride or iodide salt of so serum, contain oxidizable substrate and other ingredi dium, potassium, ammonium, calcium or magnesium or ents which undergo an enzymatic reaction in the pres mixtures of such salts. ence of oxidoreductase enzyme speci?c to the substrate The oxidizable substrate is generally present in the to produce hydrogen peroxide. oxidoreductase en enzymatic absorbent material in an amount from about zymes which can be utilized in the practice of this in 0.015 to about 0.6 millimole per gram of material and, vention and the corresponding oxidizable substrates in preferably, in an amount from about 0.025 to about 0.1 serum are set forth in the following table: millimole per gram of material.
Recommended publications
  • Non-Homologous Isofunctional Enzymes: a Systematic Analysis Of
    Omelchenko et al. Biology Direct 2010, 5:31 http://www.biology-direct.com/content/5/1/31 RESEARCH Open Access Non-homologousResearch isofunctional enzymes: A systematic analysis of alternative solutions in enzyme evolution Marina V Omelchenko, Michael Y Galperin*, Yuri I Wolf and Eugene V Koonin Abstract Background: Evolutionarily unrelated proteins that catalyze the same biochemical reactions are often referred to as analogous - as opposed to homologous - enzymes. The existence of numerous alternative, non-homologous enzyme isoforms presents an interesting evolutionary problem; it also complicates genome-based reconstruction of the metabolic pathways in a variety of organisms. In 1998, a systematic search for analogous enzymes resulted in the identification of 105 Enzyme Commission (EC) numbers that included two or more proteins without detectable sequence similarity to each other, including 34 EC nodes where proteins were known (or predicted) to have distinct structural folds, indicating independent evolutionary origins. In the past 12 years, many putative non-homologous isofunctional enzymes were identified in newly sequenced genomes. In addition, efforts in structural genomics resulted in a vastly improved structural coverage of proteomes, providing for definitive assessment of (non)homologous relationships between proteins. Results: We report the results of a comprehensive search for non-homologous isofunctional enzymes (NISE) that yielded 185 EC nodes with two or more experimentally characterized - or predicted - structurally unrelated proteins. Of these NISE sets, only 74 were from the original 1998 list. Structural assignments of the NISE show over-representation of proteins with the TIM barrel fold and the nucleotide-binding Rossmann fold. From the functional perspective, the set of NISE is enriched in hydrolases, particularly carbohydrate hydrolases, and in enzymes involved in defense against oxidative stress.
    [Show full text]
  • Increased Whitening Efficacy and Reduced Cytotoxicity Are Achieved by the Chemical Activation of a Highly Concentrated Hydrogen Peroxide Bleaching Gel
    Original Article http://dx.doi.org/10.1590/1678-7757-2018-0453 Increased whitening efficacy and reduced cytotoxicity are achieved by the chemical activation of a highly concentrated hydrogen peroxide bleaching gel Abstract Diana Gabriela SOARES1 Objective: This study was designed for the chemical activation of a 35% hydrogen peroxide (H O ) bleaching gel to increase its whitening effectiveness Natália MARCOMINI² 2 2 and reduce its toxicity. Methodology: First, the bleaching gel - associated or Carla Caroline de Oliveira DUQUE³ not with ferrous sulfate (FS), manganese chloride (MC), peroxidase (PR), Ester Alves Ferreira BORDINI³ or catalase (CT) - was applied (3x 15 min) to enamel/dentin discs adapted Uxua Ortecho ZUTA³ to artificial pulp chambers. Then, odontoblast-like MDPC-23 cells were Fernanda Gonçalves BASSO⁴ exposed for 1 h to the extracts (culture medium + components released Josimeri HEBLING⁵ from the product), for the assessment of viability (MTT assay) and oxidative D Carlos Alberto de Souza COSTA⁴ stress (H2DCFDA). Residual H2O2 and bleaching effectiveness ( E) were also evaluated. Data were analyzed with one-way ANOVA complemented with Tukey’s test (n=8. p<0.05). Results: All chemically activated groups minimized MDPC-23 oxidative stress generation; however, significantly higher cell viability was detected for MC, PR, and CT than for plain 35% H2O2 gel. Nevertheless, FS, MC, PR, and CT reduced the amount of residual H2O2 and increased bleaching effectiveness. Conclusion: Chemical activation of 35% H2O2 gel with MC, PR, and CT minimized residual H2O2 and pulp cell toxicity; but PR duplicated the whitening potential of the bleaching gel after a single 45-minute session.
    [Show full text]
  • Chloride Peroxidase Cat
    chloride peroxidase Cat. No. EXWM-0491 Lot. No. (See product label) Introduction Description Brings about the chlorination of a range of organic molecules, forming stable C-Cl bonds. Also oxidizes bromide and iodide. Enzymes of this type are either heme-thiolate proteins, or contain vanadate. A secreted enzyme produced by the ascomycetous fungus Caldariomyces fumago (Leptoxyphium fumago) is an example of the heme-thiolate type. It catalyses the production of hypochlorous acid by transferring one oxygen atom from H2O2 to chloride. At a separate site it catalyses the chlorination of activated aliphatic and aromatic substrates, via HClO and derived chlorine species. In the absence of halides, it shows peroxidase (e.g. phenol oxidation) and peroxygenase activities. The latter inserts oxygen from H2O2 into, for example, styrene (side chain epoxidation) and toluene (benzylic hydroxylation), however, these activities are less pronounced than its activity with halides. Has little activity with non-activated substrates such as aromatic rings, ethers or saturated alkanes. The chlorinating peroxidase produced by ascomycetous fungi (e.g. Curvularia inaequalis) is an example of a vanadium chloroperoxidase, and is related to bromide peroxidase (EC 1.11.1.18). It contains vanadate and oxidizes chloride, bromide and iodide into hypohalous acids. In the absence of halides, it peroxygenates organic sulfides and oxidizes ABTS [2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonic acid)] but no phenols. Synonyms chloroperoxidase; CPO; vanadium haloperoxidase Product Information Form Liquid or lyophilized powder EC Number EC 1.11.1.10 CAS No. 9055-20-3 Reaction RH + chloride + H2O2 = RCl + 2 H2O Notes This item requires custom production and lead time is between 5-9 weeks.
    [Show full text]
  • Chloroperoxidase Generation of Singlet a Molecular Oxygen
    Proc. Natl. Acad. Sci. USA Vol. 80, pp. 5195-5197, September 1983 Biochemistry Chloroperoxidase generation of singlet A molecular oxygen observed directly by spectroscopy in the 1- to 1.6-pm region [(0,0) transition/chloride peroxidase/hydrogen peroxide/chloride ion] AHSAN U. KHAN*, PETER GEBAUERt, AND LOWELL P. HAGERt *Institute of Molecular Biophysics and Department of Chemistry, Florida State University, Tallahassee, Florida 32306; and tDepartment of Biochemistry, University of Illinois at Urbana-Champaign, Urbana, Illinois 61801 Communicated by-Michael Kasha, May 9; 1983 ABSTRACT The (0,o) 'Ag -* 3 singlet molecular oxygen ,.um region and based on a lead sulfide detector and the other, chemiluminescence emission from a biological reaction system-, a more sensitive- germanium photodiode detector, operating chloroperoxidase (EC 1.11.1.10) acting on hydrogen peroxide at between 1.00 and 1.60 Am. The advent of this instrumentation low pH (phosphate buffer, pH 1.85) with C¢1 as a cosubstirate, was (1-3) has opened up a window on the near-infrared spectral re- recorded with an ultrasensitive IR spectrometer. The strong gion so that luminescence studies of reactions suspected of chemiluminescence emission peak observed at 1.30 ,um provides generating intermediates with (possibly very weak) near-in- clear evidence of the enzymatic generation of (excited) singlet ox- frared emission can now be monitored directly, as has been done ygen from peroxide in this system. successfully with photosensitization by dye (1) and superoxide anion disproportionation (3). The present work used-the liquid The observation of 'Ag -- -' singlet molecular oxygen chemi- nitrogen-cooled photovoltaic intrinsic germanium detector, which luminescence emission generated by the chloroperoxidase- is described elsewhere (3).
    [Show full text]
  • New Automatically Built Profiles for a Better Understanding of the Peroxidase Superfamily Evolution
    University of Geneva Practical training report submitted for the Master Degree in Proteomics and Bioinformatics New automatically built profiles for a better understanding of the peroxidase superfamily evolution presented by Dominique Koua Supervisors: Dr Christophe DUNAND Dr Nicolas HULO Laboratory of Plant Physiology, Dr Christian J.A. SIGRIST University of Geneva Swiss Institute of Bioinformatics PROSITE group. Geneva, April, 18th 2008 Abstract Motivation: Peroxidases (EC 1.11.1.x), which are encoded by small or large multigenic families, are involved in several important physiological and developmental processes. These proteins are extremely widespread and present in almost all living organisms. An important number of haem and non-haem peroxidase sequences are annotated and classified in the peroxidase database PeroxiBase (http://peroxibase.isb-sib.ch). PeroxiBase contains about 5800 peroxidase sequences classified as haem peroxidases and non-haem peroxidases and distributed between thirteen superfamilies and fifty subfamilies, (Passardi et al., 2007). However, only a few classification tools are available for the characterisation of peroxidase sequences: InterPro motifs, PRINTS and specifically designed PROSITE profiles. However, these PROSITE profiles are very global and do not allow the differenciation between very close subfamily sequences nor do they allow the prediction of specific cellular localisations. Due to the rapid growth in the number of available sequences, there is a need for continual updates and corrections of peroxidase protein sequences as well as for new tools that facilitate acquisition and classification of existing and new sequences. Currently, the PROSITE generalised profile building manner and their usage do not allow the differentiation of sequences from subfamilies showing a high degree of similarity.
    [Show full text]
  • Springer Handbook of Enzymes
    Dietmar Schomburg and Ida Schomburg (Eds.) Springer Handbook of Enzymes Volume 25 Class 1 • Oxidoreductases X EC 1.9-1.13 co edited by Antje Chang Second Edition 4y Springer Index of Recommended Enzyme Names EC-No. Recommended Name Page 1.13.11.50 acetylacetone-cleaving enzyme 673 1.10.3.4 o-aminophenol oxidase 149 1.13.12.12 apo-/?-carotenoid-14',13'-dioxygenase 732 1.13.11.34 arachidonate 5-lipoxygenase 591 1.13.11.40 arachidonate 8-lipoxygenase 627 1.13.11.31 arachidonate 12-lipoxygenase 568 1.13.11.33 arachidonate 15-lipoxygenase 585 1.13.12.1 arginine 2-monooxygenase 675 1.13.11.13 ascorbate 2,3-dioxygenase 491 1.10.2.1 L-ascorbate-cytochrome-b5 reductase 79 1.10.3.3 L-ascorbate oxidase 134 1.11.1.11 L-ascorbate peroxidase 257 1.13.99.2 benzoate 1,2-dioxygenase (transferred to EC 1.14.12.10) 740 1.13.11.39 biphenyl-2,3-diol 1,2-dioxygenase 618 1.13.11.22 caffeate 3,4-dioxygenase 531 1.13.11.16 3-carboxyethylcatechol 2,3-dioxygenase 505 1.13.11.21 p-carotene 15,15'-dioxygenase (transferred to EC 1.14.99.36) 530 1.11.1.6 catalase 194 1.13.11.1 catechol 1,2-dioxygenase 382 1.13.11.2 catechol 2,3-dioxygenase 395 1.10.3.1 catechol oxidase 105 1.13.11.36 chloridazon-catechol dioxygenase 607 1.11.1.10 chloride peroxidase 245 1.13.11.49 chlorite O2-lyase 670 1.13.99.4 4-chlorophenylacetate 3,4-dioxygenase (transferred to EC 1.14.12.9) .
    [Show full text]
  • Subcellular Structure of Bovine Thyroid Gland the LOCALIZATION of the PEROXIDASE ACTIVITY in BOVINE THYROID
    Biochem. J. (1978) 174, 939-949 939 Printed in Great Britain Subcellular Structure of Bovine Thyroid Gland THE LOCALIZATION OF THE PEROXIDASE ACTIVITY IN BOVINE THYROID By MARC J. S. DE WOLF, ALBERT R. LAGROU and HERWIG J. J. HILDERSON RUCA Laboratoryfor Human Biochemistry, University ofAntwerp and GUIDO A. F. VAN DESSEL and WILFRIED S. H. DIERICK UIA Laboratoryfor Pathological Biochemistry, University ofAntwerp, Groenenborgerlaan 171, B2020 Antwerp, Belgium (Received 27 February 1978) 1. After differential pelleting of bovine thyroid tissue the highest relative specific activities for plasma membrane markers are found in the L fraction whereas those for peroxidase activities (p-phenylenediamine, guaiacol and 3,3'-diaminobenzidine tetrachloride per- oxidases) are found in the M fraction. 2. When M+L fractions were subjected to buoyant- density equilibration in a HS zonal rotor all peroxidases show different profiles. The guaiacol peroxidase activity always follows the distribution of glucose 6-phosphatase. 3. When a Sb fraction is subjected to Sepharose 2B chromatography three major peaks are obtained. The first, eluted at the void volume, consists of membranous material and contains most of the guaiacol peroxidase activity. Most of the protein (probably thyro- globulin) is eluted with the second peak. Solubilized enzymes are recovered in the third peak. 4.p-Phenylenediamine peroxidase activity penetrates into the gel on polyacrylamide- gel electrophoresis, whereas guaiacol peroxidase activity remains at the sample zone. 5. DEAE-Sephadex A-50 chromatography resolves the peroxidase activities into two peaks, displaying different relative amounts of the different enzymic activities in each peak. 6. The peroxidase activities may be due to the presence of different proteins.
    [Show full text]
  • Characterisation, Classification and Conformational Variability Of
    Characterisation, Classification and Conformational Variability of Organic Enzyme Cofactors Julia D. Fischer European Bioinformatics Institute Clare Hall College University of Cambridge A thesis submitted for the degree of Doctor of Philosophy 11 April 2011 This dissertation is the result of my own work and includes nothing which is the outcome of work done in collaboration except where specifically indicated in the text. This dissertation does not exceed the word limit of 60,000 words. Acknowledgements I would like to thank all the members of the Thornton research group for their constant interest in my work, their continuous willingness to answer my academic questions, and for their company during my time at the EBI. This includes Saumya Kumar, Sergio Martinez Cuesta, Matthias Ziehm, Dr. Daniela Wieser, Dr. Xun Li, Dr. Irene Pa- patheodorou, Dr. Pedro Ballester, Dr. Abdullah Kahraman, Dr. Rafael Najmanovich, Dr. Tjaart de Beer, Dr. Syed Asad Rahman, Dr. Nicholas Furnham, Dr. Roman Laskowski and Dr. Gemma Holli- day. Special thanks to Asad for allowing me to use early development versions of his SMSD software and for help and advice with the KEGG API installation, to Roman for knowing where to find all kinds of data, to Dani for help with R scripts, to Nick for letting me use his E.C. tree program, to Tjaart for python advice and especially to Gemma for her constant advice and feedback on my work in all aspects, in particular the chemistry side. Most importantly, I would like to thank Prof. Janet Thornton for giving me the chance to work on this project, for all the time she spent in meetings with me and reading my work, for sharing her seemingly limitless knowledge and enthusiasm about the fascinating world of enzymes, and for being such an experienced and motivational advisor.
    [Show full text]
  • IIIHIII III US005453284A United States Patent (19) 11 Patent Number: 5,453,284 Pelico (45) Date of Patent: * Sep
    IIIHIII III US005453284A United States Patent (19) 11 Patent Number: 5,453,284 Pelico (45) Date of Patent: * Sep. 26, 1995 (54. STABILIZED ENZYMATIC DENTIFRICE 4,178,362. 12/1979 Hoogendoorn ............................ 424/48 4,269,822 5/1981 Pellico ........ ... 424/50 (76 Inventor: Michael A. Pelico, 3024 Military Ave., 4,537,764 8/1985 Pellico ... ... 424/50 Los Angeles, Calif. 90272 4,564,519 1/1986 Pellico ........ ... 424/48 4,576,817 3/1986 Montgomery ... 424/94. *ck Notice:- - - S. t s s 4,617,1904,578.265 10/19863/1986 PellicoMontgomery ........ ... ... 426/61424/50 subsequent to Aug. 9, aSOeel C1S- 5,176,899 1/1993 Montgomery ............................. 424/50 claimed. Primary Examiner-Phelan, D. Gabrielle (21 Appl. No.: 283,816 Attorney, Agent, or Firm-Donald Diamond 22 Filed: Aug. 1, 1994 (57 ABSTRACT Related U.S. Application Data Hydro-activated and/or oxygen activated aqueous, enzy matic, antimicrobial dentifrices are stabilized against enzy 63 Continuation-in-part of Ser. No. 10,841, Jan. 29, 1993, Pat. matic activation prior to oral application of the dentifrice by No. 5,336,494. incorporating a thickener into the dentifrice formulation so I51) int. Cl. ....................... A61K 128 as to provide the formulation with an enzyme immobilizing 52) U.S. Cl 424/94. 4:424/49: 424/50: viscosity which inhibits enzymatic action during processing 424/94.1: 424/94.2 and in the dentifrice package. An illustrative, thickened, - A enzymatic dentifrice with this enhancement contains glu 58 Field of Search ................................... 424/94.1-94.4, cose oxidase, glucose, lactoperoxidase and potassium thio 424/49, 50 cyanate together with carboxymethylcellulose in an amount 56) References Cited tO provide the dentifrice with a viscosity of at least about 800 centipoises.
    [Show full text]
  • Resonance Raman Spectra of Chloroperoxidase Reaction Intermediates
    Virginia Commonwealth University VCU Scholars Compass Theses and Dissertations Graduate School 1992 Resonance Raman spectra of chloroperoxidase reaction intermediates Ann Marie G. Sullivan Follow this and additional works at: https://scholarscompass.vcu.edu/etd Part of the Chemistry Commons © The Author Downloaded from https://scholarscompass.vcu.edu/etd/5610 This Dissertation is brought to you for free and open access by the Graduate School at VCU Scholars Compass. It has been accepted for inclusion in Theses and Dissertations by an authorized administrator of VCU Scholars Compass. For more information, please contact [email protected]. College of Humanities and Sciences Virginia Commonwealth University This is to certify that the dissertation prepared by Ann Marie Sullivan entitled "Resonance Raman Spectra of Chloroperoxidase Reaction Intermediates" has been approved by her committee as satisfactory completion of the dissertation requirement for the degree of Doctor of Philosophy in Chemistry. !f-�-" • • I " I I I � •• • Dare @Ann Marie G. Sullivan 1992 All Rights Reserved RESONANCE RAMAN SPECTRA OF CHLOROPEROXIDASE REACTION INTERMEDIATES A dissertation submitted in partial fulfillment of the requirements for the degree of Doctor of Philosophy in Chemistry at Virginia Commonwealth University. By Ann Marie G. Sullivan B.s. Chemistry, 1982 Virginia Polytechnic Institute and State University Director: Dr. James Terner Associate Professor Department of Chemistry Virginia Commonwealth University Richmond, Virginia December, 1992 11 To David
    [Show full text]
  • Involvement of Glutathione Peroxidases in the Occurrence And
    Zhang et al. J Transl Med (2020) 18:247 https://doi.org/10.1186/s12967-020-02420-x Journal of Translational Medicine REVIEW Open Access Involvement of glutathione peroxidases in the occurrence and development of breast cancers Man‑Li Zhang1†, Hua‑Tao Wu2†, Wen‑Jia Chen1,3, Ya Xu1, Qian‑Qian Ye1,3, Jia‑Xin Shen4 and Jing Liu1,3* Abstract Glutathione peroxidases (GPxs) belong to a family of enzymes that is important in organisms; these enzymes pro‑ mote hydrogen peroxide metabolism and protect cell membrane structure and function from oxidative damage. Based on the establishment and development of the theory of the pathological roles of free radicals, the role of GPxs has gradually attracted researchers’ attention, and the involvement of GPxs in the occurrence and development of malignant tumors has been shown. On the other hand, the incidence of breast cancer in increasing, and breast cancer has become the leading cause of cancer‑related death in females worldwide; breast cancer is thought to be related to the increased production of reactive oxygen species, indicating the involvement of GPxs in these processes. Therefore, this article focused on the molecular mechanism and function of GPxs in the occurrence and development of breast cancer to understand their role in breast cancer and to provide a new theoretical basis for the treatment of breast cancer. Keywords: Glutathione peroxidase, Breast cancer, Reactive oxygen species, Occurrence Background [4]. However, the mechanisms of the occurrence, devel- Breast cancer has become the most common cancer and opment, and metastasis of breast cancer are very com- the leading cause of cancer-related deaths in females plicated and overlap, suggesting the necessity of diferent worldwide, according to a status report on the global therapies to treat diferent subtypes of breast cancer.
    [Show full text]
  • Prediction of Activity Spectra for Substances of Bioactive Compounds of Garlic (Allium Sativum L.)
    bioRxiv preprint doi: https://doi.org/10.1101/2021.07.18.452815; this version posted July 19, 2021. The copyright holder for this preprint (which was not certified by peer review) is the author/funder, who has granted bioRxiv a license to display the preprint in perpetuity. It is made available under aCC-BY-NC 4.0 International license. ARTICLE Open access in silico tools to predict the ADMET profiling and PASS (Prediction of Activity Spectra for Substances of Bioactive compounds of Garlic (Allium sativum L.) Ivan Vito Ferrari, 1 1. Department of Industrial Engineering and LIME Laboratory, University of Rome Tor Vergata, Via del Politecnico 1, 00133 Rome, Italy; [email protected] (I.V.F.) *Corresponding Author: [email protected] Graphical abstract Keywords: in silico; ADMET; drug; open access; prediction; PASS Online ( (Prediction of Activity Spectra for Substances) , Garlic Compounds; S-allylcysteine ( SAC) and S-allylmercaptocysteine (SAMC) Abstract Background: Garlic (Allium sativum L.) is a common spice with many health benefits, mainly due to its diverse bioactive compounds, (see below) such as organic sulphides, saponins, phenolic compounds, and polysaccharides. Several studies have demonstrated its functions such as anti- inflammatory, antibacterial, and antiviral, antioxidant, cardiovascular protective and anticancer bioRxiv preprint doi: https://doi.org/10.1101/2021.07.18.452815; this version posted July 19, 2021. The copyright holder for this preprint (which was not certified by peer review) is the author/funder, who has granted bioRxiv a license to display the preprint in perpetuity. It is made available under aCC-BY-NC 4.0 International license.
    [Show full text]