A Novel, Low Power Biosensor for Real Time Monitoring of Creatinine and Urea in Peritoneal Dialysis
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Supplemental Methods
Supplemental Methods: Sample Collection Duplicate surface samples were collected from the Amazon River plume aboard the R/V Knorr in June 2010 (4 52.71’N, 51 21.59’W) during a period of high river discharge. The collection site (Station 10, 4° 52.71’N, 51° 21.59’W; S = 21.0; T = 29.6°C), located ~ 500 Km to the north of the Amazon River mouth, was characterized by the presence of coastal diatoms in the top 8 m of the water column. Sampling was conducted between 0700 and 0900 local time by gently impeller pumping (modified Rule 1800 submersible sump pump) surface water through 10 m of tygon tubing (3 cm) to the ship's deck where it then flowed through a 156 µm mesh into 20 L carboys. In the lab, cells were partitioned into two size fractions by sequential filtration (using a Masterflex peristaltic pump) of the pre-filtered seawater through a 2.0 µm pore-size, 142 mm diameter polycarbonate (PCTE) membrane filter (Sterlitech Corporation, Kent, CWA) and a 0.22 µm pore-size, 142 mm diameter Supor membrane filter (Pall, Port Washington, NY). Metagenomic and non-selective metatranscriptomic analyses were conducted on both pore-size filters; poly(A)-selected (eukaryote-dominated) metatranscriptomic analyses were conducted only on the larger pore-size filter (2.0 µm pore-size). All filters were immediately submerged in RNAlater (Applied Biosystems, Austin, TX) in sterile 50 mL conical tubes, incubated at room temperature overnight and then stored at -80oC until extraction. Filtration and stabilization of each sample was completed within 30 min of water collection. -
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bioRxiv preprint doi: https://doi.org/10.1101/527234; this version posted January 23, 2019. The copyright holder for this preprint (which was not certified by peer review) is the author/funder. All rights reserved. No reuse allowed without permission. Characterization of a thaumarchaeal symbiont that drives incomplete nitrification in the tropical sponge Ianthella basta Florian U. Moeller1, Nicole S. Webster2,3, Craig W. Herbold1, Faris Behnam1, Daryl Domman1, 5 Mads Albertsen4, Maria Mooshammer1, Stephanie Markert5,8, Dmitrij Turaev6, Dörte Becher7, Thomas Rattei6, Thomas Schweder5,8, Andreas Richter9, Margarete Watzka9, Per Halkjaer Nielsen4, and Michael Wagner1,* 1Division of Microbial Ecology, Department of Microbiology and Ecosystem Science, University of Vienna, 10 Austria. 2Australian Institute of Marine Science, Townsville, Queensland, Australia. 3 Australian Centre for Ecogenomics, School of Chemistry and Molecular Biosciences, University of 15 Queensland, St Lucia, QLD, Australia 4Center for Microbial Communities, Department of Chemistry and Bioscience, Aalborg University, 9220 Aalborg, Denmark. 20 5Institute of Marine Biotechnology e.V., Greifswald, Germany 6Division of Computational Systems Biology, Department of Microbiology and Ecosystem Science, University of Vienna, Austria. 25 7Institute of Microbiology, Microbial Proteomics, University of Greifswald, Greifswald, Germany 8Institute of Pharmacy, Pharmaceutical Biotechnology, University of Greifswald, Greifswald, Germany 9Division of Terrestrial Ecosystem Research, Department of Microbiology and Ecosystem Science, 30 University of Vienna, Austria. *Corresponding author: Michael Wagner, Department of Microbiology and Ecosystem Science, Althanstrasse 14, University of Vienna, 1090 Vienna, Austria. Email: wagner@microbial- ecology.net 1 bioRxiv preprint doi: https://doi.org/10.1101/527234; this version posted January 23, 2019. The copyright holder for this preprint (which was not certified by peer review) is the author/funder. -
Chemical Transformations Encoded by a Gene Cluster in Streptomyces Coelicolor Containing an Unusual Gtp Cyclohydrolase
Chemical Transformations Encoded by a Streptomyces coelicolor Gene Cluster with an Unusual GTP Cyclohydrolase Item Type text; Electronic Dissertation Authors Spoonamore, James Edward Publisher The University of Arizona. Rights Copyright © is held by the author. Digital access to this material is made possible by the University Libraries, University of Arizona. Further transmission, reproduction or presentation (such as public display or performance) of protected items is prohibited except with permission of the author. Download date 11/10/2021 06:44:52 Link to Item http://hdl.handle.net/10150/194825 CHEMICAL TRANSFORMATIONS ENCODED BY A GENE CLUSTER IN STREPTOMYCES COELICOLOR CONTAINING AN UNUSUAL GTP CYCLOHYDROLASE by James Edward Spoonamore ______________________________ A Dissertation Submitted to the Faculty of the DEPARTMENT OF BIOCHEMISTRY AND MOLECULAR BIOPHYSICS In Partial Fulfillment of the Requirements For the Degree of DOCTOR OF PHILOSOPHY In the Graduate College THE UNIVERSITY OF ARIZONA 2008 2 THE UNIVERSITY OF ARIZONA GRADUATE COLLEGE As members of the Dissertation Committee, we certify that we have read the dissertation prepared by James Edward Spoonamore entitled Chemical Transformations Encoded by a Gene Cluster in Streptomyces coelicolor Containing an Unusual GTP Cyclohydrolase and recommend that it be accepted as fulfilling the dissertation requirement for the Degree of Doctor of Philosophy _______________________________________________________________________ Date: April 16, 2008 Vahe Bandarian _______________________________________________________________________ -
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Lawrence Berkeley National Laboratory Recent Work Title A subset of the diverse COG0523 family of putative metal chaperones is linked to zinc homeostasis in all kingdoms of life. Permalink https://escholarship.org/uc/item/0f2815fq Journal BMC genomics, 10(1) ISSN 1471-2164 Authors Haas, Crysten E Rodionov, Dmitry A Kropat, Janette et al. Publication Date 2009-10-12 DOI 10.1186/1471-2164-10-470 Peer reviewed eScholarship.org Powered by the California Digital Library University of California BMC Genomics BioMed Central Research article Open Access A subset of the diverse COG0523 family of putative metal chaperones is linked to zinc homeostasis in all kingdoms of life Crysten E Haas1, Dmitry A Rodionov2,3, Janette Kropat4, Davin Malasarn4, Sabeeha S Merchant4 and Valérie de Crécy-Lagard*1 Address: 1Department of Microbiology and Cell Science, University of Florida, Gainesville, FL, USA, 2Burnham Institute for Medical Research, La Jolla, CA, USA, 3Institute for Information Transmission Problems (the Kharkevich Institute), RAS, Moscow, Russia and 4Department of Chemistry and Biochemistry and Institute for Genomics and Proteomics, University of California at Los Angeles, Los Angeles, CA, USA Email: Crysten E Haas - [email protected]; Dmitry A Rodionov - [email protected]; Janette Kropat - [email protected]; Davin Malasarn - [email protected]; Sabeeha S Merchant - [email protected]; Valérie de Crécy-Lagard* - [email protected] * Corresponding author Published: 12 October 2009 Received: 25 June 2009 Accepted: 12 October 2009 BMC Genomics 2009, 10:470 doi:10.1186/1471-2164-10-470 This article is available from: http://www.biomedcentral.com/1471-2164/10/470 © 2009 Haas et al; licensee BioMed Central Ltd. -
Subject Index Proc
13088 Subject Index Proc. Natl. Acad. Sci. USA 91 (1994) Apoptosis in substantia nigra following developmental striatal excitotoxic Brine shrimp injury, 8117 See Artemia Visualizing hippocampal synaptic function by optical detection of Ca2l Broccol entry through the N-methyl-D-aspartate channel, 8170 See Brassica Amygdala modulation of hippocampal-dependent and caudate Bromophenacyl bromide nucleus-dependent memory processes, 8477 Bromophenacyl bromide binding to the actin-bundling protein I-plastin Distribution of corticotropin-releasing factor receptor mRNA expression inhibits inositol trisphosphate-independent increase in Ca2l in human in the rat brain and pituitary, 8777 neutrophils, 3534 Brownian dynamics Preproenkephalin promoter yields region-specific and long-term Adhesion of hard spheres under the influence of double-layer, van der expression in adult brain after direct in vivo gene transfer via a Waals, and gravitational potentials at a solid/liquid interface, 3004 defective herpes simplex viral vector, 8979 Browsers Intravenous administration of a transferrin receptor antibody-nerve Thorn-like prickles and heterophylly in Cyanea: Adaptations to extinct growth factor conjugate prevents the degeneration of cholinergic avian browsers on Hawaii?, 2810 striatal neurons in a model of Huntington disease, 9077 Bruton agammaglobulinemia Axotomy induces the expression of vasopressin receptors in cranial and Genomic organization and structure of Bruton agammaglobulinemia spinal motor nuclei in the adult rat, 9636 tyrosine kinase: Localization -
B Number Gene Name Strand Orientation Protein Length Mrna
list list sample) short list predicted B number Operon ID Gene name assignment Protein length mRNA present mRNA intensity Gene description Protein detected - Strand orientation Membrane protein detected (total list) detected (long list) membrane sample Proteins detected - detected (short list) # of tryptic peptides # of tryptic peptides # of tryptic peptides # of tryptic peptides # of tryptic peptides Functional category detected (membrane Protein detected - total Protein detected - long b0001 thrL + 21 1344 P 1 0 0 0 0 thr operon leader peptide Metabolism of small molecules 1 b0002 thrA + 820 13624 P 39 P 18 P 18 P 18 P(m) 2 aspartokinase I, homoserine dehydrogenase I Metabolism of small molecules 1 b0003 thrB + 310 6781 P 9 P 3 3 P 3 0 homoserine kinase Metabolism of small molecules 1 b0004 thrC + 428 15039 P 18 P 10 P 11 P 10 0 threonine synthase Metabolism of small molecules 1 b0005 b0005 + 98 432 A 5 0 0 0 0 orf, hypothetical protein Open reading frames 2 b0006 yaaA - 258 1047 P 11 P 1 2 P 1 0 orf, hypothetical protein Open reading frames 3 b0007 yaaJ - 476 342 P 8 0 0 0 0 MP-GenProt-PHD inner membrane transport protein Miscellaneous 4 b0008 talB + 317 20561 P 20 P 13 P 16 P 13 0 transaldolase B Metabolism of small molecules 5 b0009 mog + 195 1296 P 7 0 0 0 0 required for the efficient incorporation of molybdate into molybdoproteins Metabolism of small molecules 6 b0010 yaaH - 188 407 A 2 0 0 0 0 PHD orf, hypothetical protein Open reading frames 7 b0011 b0011 - 237 338 P 13 0 0 0 0 putative oxidoreductase Miscellaneous 8 b0012 htgA -
Microbial Enzymes: Industrial Progress in 21St Century
3 Biotech (2016) 6:174 DOI 10.1007/s13205-016-0485-8 REVIEW ARTICLE Microbial enzymes: industrial progress in 21st century 1 1 2 3 Rajendra Singh • Manoj Kumar • Anshumali Mittal • Praveen Kumar Mehta Received: 8 April 2016 / Accepted: 1 August 2016 Ó The Author(s) 2016. This article is published with open access at Springerlink.com Abstract Biocatalytic potential of microorganisms have Introduction been employed for centuries to produce bread, wine, vinegar and other common products without understanding Microbes have been utilized since ancient human civi- the biochemical basis of their ingredients. Microbial lization with first reported commercial application of yeast enzymes have gained interest for their widespread uses in to produce alcoholic beverages from barley by the Baby- industries and medicine owing to their stability, catalytic lonians and Sumerians as early as 6000 BC. The microbial activity, and ease of production and optimization than plant enzymes have gained recognition globally for their wide- and animal enzymes. The use of enzymes in various spread uses in various sectors of industries, e.g., food, industries (e.g., food, agriculture, chemicals, and pharma- agriculture, chemicals, medicine, and energy. Enzyme ceuticals) is increasing rapidly due to reduced processing mediated processes are rapidly gaining interest because of time, low energy input, cost effectiveness, nontoxic and reduced process time, intake of low energy input, cost eco-friendly characteristics. Microbial enzymes are capable effective, nontoxic and eco-friendly characteristics (Li of degrading toxic chemical compounds of industrial and et al. 2012; Choi et al. 2015). Moreover, with the advent of domestic wastes (phenolic compounds, nitriles, amines recombinant DNA technology and protein engineering a etc.) either via degradation or conversion. -
Mcqs in BIOCHEMISTRY
This page intentionally left blank Copyright © 2008, New Age International (P) Ltd., Publishers Published by New Age International (P) Ltd., Publishers All rights reserved. No part of this ebook may be reproduced in any form, by photostat, microfilm, xerography, or any other means, or incorporated into any information retrieval system, electronic or mechanical, without the written permission of the publisher. All inquiries should be emailed to [email protected] ISBN (13) : 978-81-224-2627-4 PUBLISHING FOR ONE WORLD NEW AGE INTERNATIONAL (P) LIMITED, PUBLISHERS 4835/24, Ansari Road, Daryaganj, New Delhi - 110002 Visit us at www.newagepublishers.com Dedicated to PROF. DR. F.V. MANVI SecretarySecretarySecretary KLE Society, BELGAUM KARNATAKA. “To My First Pharmacy teacher with Love” This page intentionally left blank FOREWORD Competitive Examinations are the order of the day. All Colleges conducting professional courses at PG level are admitting students based on common entrance examination, which is of objective type. In Pharmacy, M.Pharm admissions are based on qualifying the GATE enterance examination conducted by Govt. of India. In this book, The author has done good work in preparing several objective questions which help the students to face the subject in the examination with poise and confidence. The book is well balanced and consists of multiple choice questions from all the important topics like carbohydrate metabolism and other important Biochemical aspects. The typesetting and quality of printing is good. The author is also well experienced in taking up this type of work. I recommend this book to all the students preparing for GATE examination and also for Medical and Pharmacy College libraries. -
Osu1056980709.Pdf (5.18
COORDINATION OF CELL CYCLE AND CELL DIFFERENTIATION BY RECEPTOR ACTIVATOR OF NF-KAPPA-B LIGAND DURING OSTEOCLAST DIFFERENTIATION DISSERTATION Presented in Partial Fulfillment of the Requirements for The Degree Doctor of Philosophy in the Graduate School of The Ohio State University By Uma Sankar ***** The Ohio State University 2003 Dissertation Committee: Approved by Professor Michael C. Ostrowski, Adviser Professor Gustavo W. Leone Adviser Professor Natarajan Muthusamy Molecular, Cellular and Professor Russell J. Hill Developmental Biology ABSTRACT Osteoclasts are bone resorbing multinuclear cells formed by the fusion of hematopoietic mononuclear precursor cells of the macrophage/monocyte lineage. Microphthalmia transcription factor (MITF) is a basic helix-loop-helix leucine zipper transcription factor that is important for the differentiation of many cell types, including osteoclasts and melanocytes. MITF regulates the expression of osteoclast-differentiation marker genes, Tartrate-resistant acid phosphatase (TRAP) and cathepsin K. Deletion in arginine 215 in the basic domain of MITF results in severe osteopetrosis in homozygous recessive mice (Mitfmi/mi). A substitution of arginine 216, in the basic domain, with lysine results in age resolving osteopetrosis in mice in the homozygous condition (Mitfor/or). However, mice that are homozygous recessive for a substitution of isoleucine to asparagine in the basic domain of this transcription factor (Mitfwh/wh) do not exhibit any osteopetrosis. We identified several novel genes regulated by Mitf with potential roles in osteoclast differentiation via microarray analysis of cDNA from WT and Mitfmi/mi osteoclasts. In particular, Eos, HOX11L2, Hematopoietic cell phosphatase (HCP) and p9 were confirmed to be expressed in lower levels in Mitfmi/mi osteoclasts compared to the WT. -
Creatinine and Urea Biosensors Based on a Novel Ammonium Ion-Selective Copper-Polyaniline Nano-Composite
CORE Metadata, citation and similar papers at core.ac.uk Provided by MURAL - Maynooth University Research Archive Library Biosensors and Bioelectronics 77 (2016) 505–511 Contents lists available at ScienceDirect Biosensors and Bioelectronics journal homepage: www.elsevier.com/locate/bios Creatinine and urea biosensors based on a novel ammonium ion-selective copper-polyaniline nano-composite M. Zhybak a,b, V. Beni b,n, M.Y. Vagin c, E. Dempsey d, A.P.F. Turner b, Y. Korpan a,n a Laboratory of Biomolecular Electronics, Institute of Molecular Biology and Genetics, National Academy of Sciences of Ukraine, 03680 Kyiv, Ukraine b Biosensors & Bioelectronics Centre, IFM, Linköping University, 58183, Sweden c Applied Physics Division, IFM, Linköping University, Linköping, 58183, Sweden d Centre for Research in Electroanalytical Technologies, Department of Science, ITT Dublin, Tallaght, Dublin 24, Ireland article info abstract Article history: The use of a novel ammonium ion-specific copper-polyaniline nano-composite as transducer for hy- Received 22 July 2015 drolase-based biosensors is proposed. In this work, a combination of creatinine deaminase and urease Received in revised form has been chosen as a model system to demonstrate the construction of urea and creatinine biosensors to 29 September 2015 illustrate the principle. Immobilisation of enzymes was shown to be a crucial step in the development of Accepted 3 October 2015 the biosensors; the use of glycerol and lactitol as stabilisers resulted in a significant improvement, Available online 9 October 2015 especially in the case of the creatinine, of the operational stability of the biosensors (from few hours to at Keywords: least 3 days). -
12) United States Patent (10
US007635572B2 (12) UnitedO States Patent (10) Patent No.: US 7,635,572 B2 Zhou et al. (45) Date of Patent: Dec. 22, 2009 (54) METHODS FOR CONDUCTING ASSAYS FOR 5,506,121 A 4/1996 Skerra et al. ENZYME ACTIVITY ON PROTEIN 5,510,270 A 4/1996 Fodor et al. MICROARRAYS 5,512,492 A 4/1996 Herron et al. 5,516,635 A 5/1996 Ekins et al. (75) Inventors: Fang X. Zhou, New Haven, CT (US); 5,532,128 A 7/1996 Eggers Barry Schweitzer, Cheshire, CT (US) 5,538,897 A 7/1996 Yates, III et al. s s 5,541,070 A 7/1996 Kauvar (73) Assignee: Life Technologies Corporation, .. S.E. al Carlsbad, CA (US) 5,585,069 A 12/1996 Zanzucchi et al. 5,585,639 A 12/1996 Dorsel et al. (*) Notice: Subject to any disclaimer, the term of this 5,593,838 A 1/1997 Zanzucchi et al. patent is extended or adjusted under 35 5,605,662 A 2f1997 Heller et al. U.S.C. 154(b) by 0 days. 5,620,850 A 4/1997 Bamdad et al. 5,624,711 A 4/1997 Sundberg et al. (21) Appl. No.: 10/865,431 5,627,369 A 5/1997 Vestal et al. 5,629,213 A 5/1997 Kornguth et al. (22) Filed: Jun. 9, 2004 (Continued) (65) Prior Publication Data FOREIGN PATENT DOCUMENTS US 2005/O118665 A1 Jun. 2, 2005 EP 596421 10, 1993 EP 0619321 12/1994 (51) Int. Cl. EP O664452 7, 1995 CI2O 1/50 (2006.01) EP O818467 1, 1998 (52) U.S. -
Genome-Scale Metabolic Network Analysis and Drug Targeting of Multi-Drug Resistant Pathogen Acinetobacter Baumannii AYE
Electronic Supplementary Material (ESI) for Molecular BioSystems. This journal is © The Royal Society of Chemistry 2017 Electronic Supplementary Information (ESI) for Molecular BioSystems Genome-scale metabolic network analysis and drug targeting of multi-drug resistant pathogen Acinetobacter baumannii AYE Hyun Uk Kim, Tae Yong Kim and Sang Yup Lee* E-mail: [email protected] Supplementary Table 1. Metabolic reactions of AbyMBEL891 with information on their genes and enzymes. Supplementary Table 2. Metabolites participating in reactions of AbyMBEL891. Supplementary Table 3. Biomass composition of Acinetobacter baumannii. Supplementary Table 4. List of 246 essential reactions predicted under minimal medium with succinate as a sole carbon source. Supplementary Table 5. List of 681 reactions considered for comparison of their essentiality in AbyMBEL891 with those from Acinetobacter baylyi ADP1. Supplementary Table 6. List of 162 essential reactions predicted under arbitrary complex medium. Supplementary Table 7. List of 211 essential metabolites predicted under arbitrary complex medium. AbyMBEL891.sbml Genome-scale metabolic model of Acinetobacter baumannii AYE, AbyMBEL891, is available as a separate file in the format of Systems Biology Markup Language (SBML) version 2. Supplementary Table 1. Metabolic reactions of AbyMBEL891 with information on their genes and enzymes. Highlighed (yellow) reactions indicate that they are not assigned with genes. No. Metabolism EC Number ORF Reaction Enzyme R001 Glycolysis/ Gluconeogenesis 5.1.3.3 ABAYE2829