DOCSLIB.ORG

Design and Development of Some Amperometric Biosensors Based on Enzymes, Antibodies and Plant Tissue

Total Page：16

File Type：pdf, Size：1020Kb

Download full-text PDF Read full-text
Design and Development of Some Amperometric Biosensors Based on Enzymes, Antibodies and Plant Tissue Design and Development of Some Amperometric Biosensors Based on Enzymes, Antibodies and Plant Tissue by Eithne Mary Dempsey A Thesis Submitted for the Degree of Doctor of Philosophy Supervised by Malcolm R. Smyth Dublin City University September 1993 Declaration I hereby certify that this material, which I now submit for assessment on the programme of study leading to the award of Ph.D is entirely my own work and has not been taken from the work of others save and to the extent that such work has been cited and acknowledged within the text of my own work. Signed: >> Date: _gvn|Ore^ /o/9/93 Eithne Dempsey For my Family and Boris iii ACKNOWLEDGEMENTS During the various stages of the research described in this thesis I received advice and help from people both in DCU and in New Mexico State University. I would like to thank in particular the following people. I would firstly like to acknowledge and thank my supervisor Prof. Malcolm Smyth for his guidance and advice during the past three years. I am also grateful to Prof. Joe Wang in New Mexico for allowing me the opportunity to work in his lab for two six month periods. A special thanks to the 'international' group there, his research students, postdocs and visiting professors for all their ideas and help, Elisa Gonzalez Romero, Mehmet Ozsoz, Ulla Wollenberger, Ardadi Eremenko, Jie Liu, Li-Huey Wu, Alex Ciszewski, Ziad Taha, Najih Naser, Julio Reviejo Garcia, Lin, Mrs. Wu, Chen, Henning and David. Thanks also to all the chemistry postgrads of DCU, in particular Malcolm's research group of new and old, Michelle O'Connor, Kamal Sagar, Kieran McLaughlin, Ellen Rohde and visiting postdocs Emmanuel Iwuoha, Beatrice Lopez Ruiz and Chi Hua, and the newer members of the group in the lab. To the technical staff Peig, Veronica, Fintan, Maurice, Teresa and Mick for all the practical and mental guidance and of course my partners in various activities(H) including sport, Catherine, Mary Mac, Maureen, Tia and Ann Sophie in Finland for all the craic and injuries.... To Prof. Richard O'Kennedy and Denise Egan for their contribution to the coumarin research in conjunction with the Biology Dept, in DCU, and Prof. David Richardson in the Botany Dept, of Trinity College for the co-operation with the lichen project. Financial support from the Institute for International Education, is gratefully acknowledged. This scholarship allowed me the opportunity to study abroad under the American Fulbright Scholarship Scheme. TABLE OF CONTENTS Page Title Page I Declaration n Dedication HI Acknowledgements IV Table of Contents V Abstract XIV CHAPTER 1 OVERVIEW OF BIOSENSORS AND THEIR APPLICATIONS 1.1. INTRODUCTION 2 1.2. MOLECULAR RECOGNITION 4 1.2.1 Enzymes as Biocatalysts for Recognition 7 1.2.2 Tissue Biocatalysts as Recognition Agents 9 1.2.3 Whole Cells as Bioaffinity Recognition Agents 10 1.2.4 Antibodies as BioafTinity Recognition Agents 12 1.2.5. Receptors as Bioaffinity Recognition Agents 15 1.3. IMMOBILISATION 17 1.3.1. Physical Methods 17 13.1.1. Adsorption 17 I.3.I.2. Entrapment within polymers/membranes 18 1.3.2. Chemical Methods 19 I.3.2.I. Glutaraldehye Crosslinking 19 1.3.3. Langmuir Blodgett/Lipid Membranes 20 1.3.4. Effects of Immobilisation on the Properties of 21 Enzymes I.3.4.I. Kinetic effects 21 1.4. TRANSDUCTION 23 1.4.1. Electrochemical Transduction 24 V Page 1.4.1.1. Amperometric Detection 24 1.4.L1.1. Types of Electrodes 26 1.4.1.1.2. Immobilisation Strategies in Amperometric 31 Biosensors 1.4.1.1.2.1. Polymer Films 31 1.4.1.1.2.2. Electropolymerisation 32 1.4.1.1.3. Tailoring Surfaces and Permselectivity 35 1.4.1.1.4. Mediation and Electron Transfer for Enzyme 37 Electrodes 1.4.1.1.4.1, First Generation Mediators 38 1.4.1.1.4.2 Second Generation Mediators 39 1.4.1.1.4.3 Third Generation Mediators 41 1.4.1.1.5. Enzymatic Amplification 44 1.4.1.2. Potentiometrie and ISFET Devices 46 1.4.2. Optical Transduction 47 1.4.3. Calorimetric Transduction 49 1.4.4. Piezoelectric Transduction 50 1.4.5. CHARACTERISATION OF BIOSENSORS 51 1.5. A PPLIC A TIO N S 53 1.5.1 Medical Applications 54 1.5.2. Food Industry 62 1.5.3. Environmental Monitoring 63 1.5.4. Industrial Applications 65 1.5.5. Biosensor Market 66 1.6. CONCLUDING REMARKS 68 1.7. BIBLIOGRAPHY 69 vi CHAPTER 2 Page THE DEVELOPMENT OF SOME ENZYME ELECTRODES BASED ON VARIOUS IMMOBILISATION TECHNIQUES 2.1. INTRODUCTION 83 2.2. DEVELOPMENT OF AN AMPEROMETRIC 83 ENZYME ELECTRODE FOR THEOPHYLLINE 2.2.1. Experimental 86 2.2.1.1. Apparatus 86 2.2.1.2. Electrode Preparation 86 2.2.1.3. Reagents 87 2.2.1.4. Procedure 87 2.2.2. Results and Discussion 87 2.2.2.1. Amperometry and Chronoamperometry 87 2.2.2.2. Optimisation of Operating Conditions 90 2.2.2.3. Flow Injection Studies 94 2.2.2.4. Interference Studies 96 2.2.3. Conclusion 97 2.3. DEVELOPMENT OF AMPEROMETRIC 98 SENSORS FOR CHOLINE, ACETYLCHOLINE AND ARSENOCHOLINE 2.3.1. Experimental 100 2.3.1.1. Apparatus 100 2.3.1.2. Reagents 100 2.3.1.3. Electrode Preparation 101 2.3.2. Results and Discussion 101 2.3.2.1. Constant Potential Measurements 101 2.3.2.2. Development of an Amperometric Sensor for 102 Choline 2.3.2.3. Development of an Arsenocholine Sensor 106 vii Page Development of an Acetylcholine Sensor 107 Cyclic Voltammetry 108 Apparent Michaelis-Menten Constants 108 Conclusion 113 A LYSINE DEHYDROGENASE-BASED 114 ELECTRODE FOR BIOSENSING OF L-LYSINE Experimental 115 Apparatus 115 Reagents 115 Electrode Preparation 116 Procedure 116 Results and Discussion 117 Batch Amperometric Experiments 117 Selectivity Experiments and Flow Injection Analysis 124 Conclusion 127 THE DEVELOPMENT OF A LACTATE SENSOR 128 BASED ON IMMOBILISED LACTATE OXIDASE IN AN ELECTROPOLYMERISED O- PHENYLENEDIAMINE FILM Experimental 130 Apparatus 130 Reagents 130 Electrode Preparation 131 Procedures 131 Results and Discussion 132 Batch Experiments 132 Row Injection Analysis 138 Conclusion 143 viii Page 2.6. CRITICAL ASSESSMENT OF IMMOBILISATION 144 TECHNIQUES FOR AMPEROMETRIC SENSORS AND THEIR CLINICAL APPLICATION BIBLIOGRAPHY 2.7. 146 C H A PTER 3 DEVELOPMENT OF TYROSINASE AND PEROXIDASE BASED AMPEROMETRIC SENSORS FOR INHIBITING COMPOUNDS IN ORGANIC PHASE AND A STUDY OF THE KINETICS OF TYROSINASE 3.1. INTRODUCTION 151 3.2. ORGANIC-PHASE BIOSENSING OF 158 INHIBITORS OF TYROSINASE AND PEROXIDASE 3.2.1. Experimental 160 3.2.1.1. Apparatus 160 3.2.1.2. Reagents 160 3.2.1.3. Procedure 160 3.2.2. Results and Discussion 161 3.2.2.1. Amperometric Batch Inhibition Measurements 161 3.2.2.2. Estimation of the Effect of Substrate Concentration 168 and Calculation of Relevant Kinetic Parameters 3.2.3.3. Flow injection Experiments 171 3.2.3. Conclusion 175 3.3. INVESTIGATION OF THE EFFECTS OF 177 VARIOUS ORGANIC SOLVENTS ON THE KINETICS AND ACTIVITY OF IMMOBILISED TYROSINASE USING THE ROTATING DISC IX ELECTRODE Page 3.3.1. Experimental 178 3.3.1.1 Apparatus 178 3.3.1.2 Reagents 178 3.3.I.3. Procedures 178 3.3.2. Results and Discussion 179 3.3.2.1. Enzyme Model 179 3.3.2.2. Rotating Disc Experiments at Constant Potential 181 3.3.2.3. Comparison of Activity in Various Organic Solvents 186 3.3.3. Conclusion 191 3.4. FUTURE POSSIBILITIES FOR ORGANIC-PHASE 192 ENZYME ELECTRODES 3.5. B IB LIO G R A PH Y 195 C H A PTER 4 DIFFERENTIAL PULSE VOLTAMMETRIC DETERMINATION OF 7-HYDROXY- COUMARIN IN HUMAN URINE AND THE DEVELOPMENT OF AN ANTIBODY-BASED AMPEROMETRIC BIOSENSOR TO STUDY ITS REACTION WITH ITS SPECIFIC ANTIBODY 4.1. INTRODUCTION 199 4.2. DIFFERENTIAL PULSE VOLTAMMETRY OF 200 7-HYDROXY-COUMARIN IN HUMAN URINE 4.2.1. Experimental 200 4.2.1.1. Apparatus 200 4.2.1.2. Electrode Preparation 201 4.2.1.3. Reagents 201 X Page 4.2.I.4. Procedures 201 4.2.L4.1. Electrochemical Behaviou of 7-OH-Coumarin 201 4.2.1.4.2. Analysis of 7-OH-Coumarin in Urine Samples 202 4.2.2. Results and Discussion 202 4.2.2.1. Anodic Voltammetric Behaviour of 7-OH-Coumarin 202 4.2.2.2. Voltammetric Determination of 7-OH-Coumarin 205 in Human Urine 4.3. DEVELOPMENT OF AN ANTIBODY-BASED 208 AMPEROMETRIC BIOSENSOR TO STUDY THE REACTION OF 7-HYDROXY-COUMARIN WITH ITS SPECIFIC ANTIBODY 4.3.1. Experimental 208 4.3.1.1. Apparatus 208 4.3.1.2. Electrode Preparation 208 4.3.1.3. Reagents 208 4.3.2. Results and Discussion 209 4.3.2.1. Electrochemical Studies on the Behaviour of 209 7-OH-Coumarin 4.3.2.2. Development of an Antibody-Based Biosensor. 209 4.4. CONCLUSION 214 4.5. FUTURE DEVELOPMENTS IN THE AREA OF 214 ANTIBODY-BASED BIOAFFINITY SENSORS 4.6. BIBLIOGRAPHY 215 C H A PTER 5 APPLICATION OF LICHEN-MODIFIED CARBON PASTE ELECTRODES FOR VOLTAMMETRIC DETERMINATION OF METAL IONS IN MULTIELEMENT AND SPECIATION STUDIES xi Page 5.1. INTRODUCTION 218 5.2. Experimental 219 5.2.1. Reagents 219 5.2.2. Apparatus 219 5.2.3. Electrode Preparation 220 5.2.4. Procedure 220 5.3. Results and Discussion 221 5.3.1. Multicomponent Analysis 221 5.3.2. Surface Renewal 223 5.3.3. Extractions 225 5.3.4. Spéciation of Cu(II) and Cu(I) 226 5.4.
Load more

Recommended publications
  • CDH12 Cadherin 12, Type 2 N-Cadherin 2 RPL5 Ribosomal
    5 6 6 5 . 4 2 1 1 1 2 4 1 1 1 1 1 1 1 1 1 1 1 1 1 1 1 1 1 1 2 2 A A A A A A A A A A A A A A A A A A A A C C C C C C C C C C C C C C C C C C C C R R R R R R R R R R R R R R R R R R R R B , B B B B B B B B B B B B B B B B B B B , 9 , , , , 4 , , 3 0 , , , , , , , , 6 2 , , 5 , 0 8 6 4 , 7 5 7 0 2 8 9 1 3 3 3 1 1 7 5 0 4 1 4 0 7 1 0 2 0 6 7 8 0 2 5 7 8 0 3 8 5 4 9 0 1 0 8 8 3 5 6 7 4 7 9 5 2 1 1 8 2 2 1 7 9 6 2 1 7 1 1 0 4 5 3 5 8 9 1 0 0 4 2 5 0 8 1 4 1 6 9 0 0 6 3 6 9 1 0 9 0 3 8 1 3 5 6 3 6 0 4 2 6 1 0 1 2 1 9 9 7 9 5 7 1 5 8 9 8 8 2 1 9 9 1 1 1 9 6 9 8 9 7 8 4 5 8 8 6 4 8 1 1 2 8 6 2 7 9 8 3 5 4 3 2 1 7 9 5 3 1 3 2 1 2 9 5 1 1 1 1 1 1 5 9 5 3 2 6 3 4 1 3 1 1 4 1 4 1 7 1 3 4 3 2 7 6 4 2 7 2 1 2 1 5 1 6 3 5 6 1 3 6 4 7 1 6 5 1 1 4 1 6 1 7 6 4 7 e e e e e e e e e e e e e e e e e e e e e e e e e e e e e e e e e e e e e e e e e e e e e e e e e e e e e e e e e e e e e e e e e e e e e e e e e e e e e e e e e e e e e e e e e e e e e e e e e e e e e e e e e e e e e e e e e e e e e l l l l l l l l l l l l l l l l l l l l l l l l l l l l l l l l l l l l l l l l l l l l l l l l l l l l l l l l l l l l l l l l l l l l l l l l l l l l l l l l l l l l l l l l l l l l l l l l l l l l l l l l l l l l l l l l l l l l l p p p p p p p p p p p p p p p p p p p p p p p p p p p p p p p p p p p p p p p p p p p p p p p p p p p p p p p p p p p p p p p p p p p p p p p p p p p p p p p p p p p p p p p p p p p p p p p p p p p p p p p p p p p p p p p p p p p p p m m m m m m m m m m m m m m m m m m m m m m m m m m m m m m m m m m m m m m m m m m m m m m m m m m m m
    [Show full text]
  • Supplementary Materials
    Supplementary Materials COMPARATIVE ANALYSIS OF THE TRANSCRIPTOME, PROTEOME AND miRNA PROFILE OF KUPFFER CELLS AND MONOCYTES Andrey Elchaninov1,3*, Anastasiya Lokhonina1,3, Maria Nikitina2, Polina Vishnyakova1,3, Andrey Makarov1, Irina Arutyunyan1, Anastasiya Poltavets1, Evgeniya Kananykhina2, Sergey Kovalchuk4, Evgeny Karpulevich5,6, Galina Bolshakova2, Gennady Sukhikh1, Timur Fatkhudinov2,3 1 Laboratory of Regenerative Medicine, National Medical Research Center for Obstetrics, Gynecology and Perinatology Named after Academician V.I. Kulakov of Ministry of Healthcare of Russian Federation, Moscow, Russia 2 Laboratory of Growth and Development, Scientific Research Institute of Human Morphology, Moscow, Russia 3 Histology Department, Medical Institute, Peoples' Friendship University of Russia, Moscow, Russia 4 Laboratory of Bioinformatic methods for Combinatorial Chemistry and Biology, Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry of the Russian Academy of Sciences, Moscow, Russia 5 Information Systems Department, Ivannikov Institute for System Programming of the Russian Academy of Sciences, Moscow, Russia 6 Genome Engineering Laboratory, Moscow Institute of Physics and Technology, Dolgoprudny, Moscow Region, Russia Figure S1. Flow cytometry analysis of unsorted blood sample. Representative forward, side scattering and histogram are shown. The proportions of negative cells were determined in relation to the isotype controls. The percentages of positive cells are indicated. The blue curve corresponds to the isotype control. Figure S2. Flow cytometry analysis of unsorted liver stromal cells. Representative forward, side scattering and histogram are shown. The proportions of negative cells were determined in relation to the isotype controls. The percentages of positive cells are indicated. The blue curve corresponds to the isotype control. Figure S3. MiRNAs expression analysis in monocytes and Kupffer cells. Full-length of heatmaps are presented.
    [Show full text]
  • Transcriptomic and Proteomic Profiling Provides Insight Into
    BASIC RESEARCH www.jasn.org Transcriptomic and Proteomic Profiling Provides Insight into Mesangial Cell Function in IgA Nephropathy † † ‡ Peidi Liu,* Emelie Lassén,* Viji Nair, Celine C. Berthier, Miyuki Suguro, Carina Sihlbom,§ † | † Matthias Kretzler, Christer Betsholtz, ¶ Börje Haraldsson,* Wenjun Ju, Kerstin Ebefors,* and Jenny Nyström* *Department of Physiology, Institute of Neuroscience and Physiology, §Proteomics Core Facility at University of Gothenburg, University of Gothenburg, Gothenburg, Sweden; †Division of Nephrology, Department of Internal Medicine and Department of Computational Medicine and Bioinformatics, University of Michigan, Ann Arbor, Michigan; ‡Division of Molecular Medicine, Aichi Cancer Center Research Institute, Nagoya, Japan; |Department of Immunology, Genetics and Pathology, Uppsala University, Uppsala, Sweden; and ¶Integrated Cardio Metabolic Centre, Karolinska Institutet Novum, Huddinge, Sweden ABSTRACT IgA nephropathy (IgAN), the most common GN worldwide, is characterized by circulating galactose-deficient IgA (gd-IgA) that forms immune complexes. The immune complexes are deposited in the glomerular mesangium, leading to inflammation and loss of renal function, but the complete pathophysiology of the disease is not understood. Using an integrated global transcriptomic and proteomic profiling approach, we investigated the role of the mesangium in the onset and progression of IgAN. Global gene expression was investigated by microarray analysis of the glomerular compartment of renal biopsy specimens from patients with IgAN (n=19) and controls (n=22). Using curated glomerular cell type–specific genes from the published literature, we found differential expression of a much higher percentage of mesangial cell–positive standard genes than podocyte-positive standard genes in IgAN. Principal coordinate analysis of expression data revealed clear separation of patient and control samples on the basis of mesangial but not podocyte cell–positive standard genes.
    [Show full text]
  • Oxidized Phospholipids Regulate Amino Acid Metabolism Through MTHFD2 to Facilitate Nucleotide Release in Endothelial Cells
    ARTICLE DOI: 10.1038/s41467-018-04602-0 OPEN Oxidized phospholipids regulate amino acid metabolism through MTHFD2 to facilitate nucleotide release in endothelial cells Juliane Hitzel1,2, Eunjee Lee3,4, Yi Zhang 3,5,Sofia Iris Bibli2,6, Xiaogang Li7, Sven Zukunft 2,6, Beatrice Pflüger1,2, Jiong Hu2,6, Christoph Schürmann1,2, Andrea Estefania Vasconez1,2, James A. Oo1,2, Adelheid Kratzer8,9, Sandeep Kumar 10, Flávia Rezende1,2, Ivana Josipovic1,2, Dominique Thomas11, Hector Giral8,9, Yannick Schreiber12, Gerd Geisslinger11,12, Christian Fork1,2, Xia Yang13, Fragiska Sigala14, Casey E. Romanoski15, Jens Kroll7, Hanjoong Jo 10, Ulf Landmesser8,9,16, Aldons J. Lusis17, 1234567890():,; Dmitry Namgaladze18, Ingrid Fleming2,6, Matthias S. Leisegang1,2, Jun Zhu 3,4 & Ralf P. Brandes1,2 Oxidized phospholipids (oxPAPC) induce endothelial dysfunction and atherosclerosis. Here we show that oxPAPC induce a gene network regulating serine-glycine metabolism with the mitochondrial methylenetetrahydrofolate dehydrogenase/cyclohydrolase (MTHFD2) as a cau- sal regulator using integrative network modeling and Bayesian network analysis in human aortic endothelial cells. The cluster is activated in human plaque material and by atherogenic lipo- proteins isolated from plasma of patients with coronary artery disease (CAD). Single nucleotide polymorphisms (SNPs) within the MTHFD2-controlled cluster associate with CAD. The MTHFD2-controlled cluster redirects metabolism to glycine synthesis to replenish purine nucleotides. Since endothelial cells secrete purines in response to oxPAPC, the MTHFD2- controlled response maintains endothelial ATP. Accordingly, MTHFD2-dependent glycine synthesis is a prerequisite for angiogenesis. Thus, we propose that endothelial cells undergo MTHFD2-mediated reprogramming toward serine-glycine and mitochondrial one-carbon metabolism to compensate for the loss of ATP in response to oxPAPC during atherosclerosis.
    [Show full text]
  • 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.
    [Show full text]
  • Properties of a Newenzyme,Nucleoside Oxidase
    Agric. Biol. Chem., 53 (6), 1671 -1677, 1989 1671 Properties of a NewEnzyme, Nucleoside Oxidase, from Pseudomonas maltophilia LB-86 Yoshikazu Isono, TomokoSudo and MasamiHoshino Biwako Research Laboratory, Otsuka Foods Co., Ltd., Karasaki, Otsu, Shiga 520-01, Japan Received January 23, 1989 Nucleoside oxidase purified from Pseudomonas maltophilia LB-86 had mol. wt. = 130.000 and was composed of one each of four non-identical subunits: subunit a, 76,000; subunit /?, 33,000; subunit y, 18,000; subunit <5, 14,000. The enzyme contains 1 mol of covalently bound FAD, 2g atoms of non- heme iron, 2 mol of labile sulfides, and 1 mol of heme per mol enzyme protein. The absorption spectrum of nucleoside oxidase had maxima 278 and 390nm, and shoulders at 343 and 450nm. The enzymecatalyzes the oxidation of various nucleosides, and the Kmvalue for inosine was 4.4 x 10"5 M. The enzyme was most active at pH 5-6, and was most stable between pH 5.0-6.0 and at temperatures below 60°C. The activity was strongly inhibited by /V-bromosuccinimide and potassium cyanide. As reported previously,1} a new enzyme oxidase was prepared from Pseudomonas maltophilia LB- catalyzed the oxidation of nucleosides without 86, as described previously.2' a requirement for an exogenous co factor. This nucleoside-oxidizing enzyme was quite dif- Assay of nucleoside oxidase activity. Enzymeactivity was assayed by measurementof oxygen uptake with an ferent from any previously reported enzymes, Oxygraph model 8 oxygen electrode (Central Kagaku Co., and thus we have designated tentatively it as Ltd.) placed in a thermostatically controlled vessel at "nucleoside oxidase." Nucleoside oxidase was 25°C.
    [Show full text]
  • An Overview of Production and Industrial Exploitation of Bacterial Laccases
    Punjab University Journal of Zoology 35(1): 147-156 (2020) https://dx.doi.org/10.17582/journal.pujz/2020.35.1.147.156 Review Article An Overview of Production and Industrial Exploitation of Bacterial Laccases Fehmina Ashraf1, Muhammad Irfan2*, Hafiz Abdullah Shakir1, Shaukat Ali3, Muhammad Khan1 1Department of Zoology, University of the Punjab new campus, Lahore, Pakistan 2Department of Biotechnology, University of Sargodha, Sargodha, Pakistan 3Department of Zoology, Government College University Lahore, Pakistan Article History Received: June 13, 2019 Abstract | Laccases (p-diphenol: oxygen oxidoreductase, EC 1.10.3.2) are multi-copper Revised: March 26, 2020 polyphenolic oxidases that oxidize many phenolic and non-phenolic aromatic compounds Accepted: June 15, 2020 such as amino or methoxy monophenols, syringaldazine, ABTS and amino or methoxy Published: June 29, 2020 monophenols. They have been depicted in various species of bacteria, plants and in different genera of fungi. Laccases have been purified by various methods. It involves in di-oxygen to Authors’ Contributions water reduction and 1e- oxidation of phenolic and its allied parts. Laccases are mostly used FA reviewed the literature and wrote the manuscript. MI su- in different industries like food, paper and pulp, pharmaceutical and textile etc. Both laccases pervised the study. HAS helped and mediators have been used in different process like delignification of pulp. Laccases from in manuscript writing. SA did bacterial species are used in dye decolouration and biobleaching processes. This review article literature survey. MK critically describes the whole overview of laccases. reviewed the dinal draft. Novelty Statement | This paper reported the updated knowledge about bacterial laccases.
    [Show full text]
  • Gene Expression Patterns Induced by HPV-16 L1 Virus-Like Particles in Leukocytes from Vaccine Recipients
    Gene Expression Patterns Induced by HPV-16 L1 Virus-Like Particles in Leukocytes from Vaccine Recipients This information is current as Alfonso J. García-Piñeres, Allan Hildesheim, Lori Dodd, of October 3, 2021. Troy J. Kemp, Jun Yang, Brandie Fullmer, Clayton Harro, Douglas R. Lowy, Richard A. Lempicki and Ligia A. Pinto J Immunol 2009; 182:1706-1729; ; doi: 10.4049/jimmunol.182.3.1706 http://www.jimmunol.org/content/182/3/1706 Downloaded from Supplementary http://www.jimmunol.org/content/suppl/2009/01/15/182.3.1706.DC1 Material http://www.jimmunol.org/ References This article cites 53 articles, 16 of which you can access for free at: http://www.jimmunol.org/content/182/3/1706.full#ref-list-1 Why The JI? Submit online. • Rapid Reviews! 30 days* from submission to initial decision • No Triage! Every submission reviewed by practicing scientists by guest on October 3, 2021 • Fast Publication! 4 weeks from acceptance to publication *average Subscription Information about subscribing to The Journal of Immunology is online at: http://jimmunol.org/subscription Permissions Submit copyright permission requests at: http://www.aai.org/About/Publications/JI/copyright.html Email Alerts Receive free email-alerts when new articles cite this article. Sign up at: http://jimmunol.org/alerts The Journal of Immunology is published twice each month by The American Association of Immunologists, Inc., 1451 Rockville Pike, Suite 650, Rockville, MD 20852 Copyright © 2009 by The American Association of Immunologists, Inc. All rights reserved. Print ISSN: 0022-1767 Online ISSN: 1550-6606. The Journal of Immunology Gene Expression Patterns Induced by HPV-16 L1 Virus-Like Particles in Leukocytes from Vaccine Recipients1 Alfonso J.
    [Show full text]
  • Functional and Structural Studies of AKR1B15 and AKR1B16: Two Novel Additions to Human and Mouse Aldo-Keto Reductase Superfamily
    ADVERTIMENT. Lʼaccés als continguts dʼaquesta tesi queda condicionat a lʼacceptació de les condicions dʼús establertes per la següent llicència Creative Commons: http://cat.creativecommons.org/?page_id=184 ADVERTENCIA. El acceso a los contenidos de esta tesis queda condicionado a la aceptación de las condiciones de uso establecidas por la siguiente licencia Creative Commons: http://es.creativecommons.org/blog/licencias/ WARNING. The access to the contents of this doctoral thesis it is limited to the acceptance of the use conditions set by the following Creative Commons license: https://creativecommons.org/licenses/?lang=en Functional and structural studies of AKR1B15 and AKR1B16: Two novel additions to human and mouse aldo-keto reductase superfamily Mem`oriapresentada per JOAN GIMENEZ´ DEJOZ per optar al Grau de Doctor en Bioqu´ımicai Biologia Molecular Treball realitzat al departament de Bioqu´ımicai Biologia Molecular de la Universitat Aut`onomade Barcelona, sota la direcci´odels Doctors SERGIO PORTE´ ORDUNA, JAUME FARRES´ VICEN´ i XAVIER PARES´ CASASAMPERA Sergio Port´eOrduna Jaume Farr´esVic´en Xavier Par´esCasasampera Joan Gim´enezDejoz Bellaterra, 17 de juny de 2016 2 Agra¨ıments En primer lloc vull agrair als caps del grup, el Dr. Jaume Farr´esi el Dr. Xavier Par´esl'oportunitat de posar un peu a la ci`encia,iniciar-me en la carrera cient´ıfica,els seus bons consells i l’obtenci´o final d'aquesta tesi. Tamb´evoldria agrair especialment a tots els ADHs amb qui he compartit laboratori, sense vosaltres aix`ono hauria estat possible. Gr`aciesper aguantar tants dies a les fosques! Al Sergio-せんせい, per tot el que m'has ensenyat durant aquests anys, la bona guia, direcci´o, les inacabables correccions, per ensenyar-me a ser cr´ıticamb la meva pr`opiafeina i intentar sempre ser rigor´osi auto exigent tant amb els experiments com amb la redacci´oi preparaci´ode les figures (repassar cada figura mil cops buscant defectes abans de donar-la per bona ja s'ha convertit en costum) i tots i cada un dels inacabables \Podries..."que tant hem trobat a faltar en la `epoca final.
    [Show full text]
  • All Enzymes in BRENDA™ the Comprehensive Enzyme Information System
    All enzymes in BRENDA™ The Comprehensive Enzyme Information System http://www.brenda-enzymes.org/index.php4?page=information/all_enzymes.php4 1.1.1.1 alcohol dehydrogenase 1.1.1.B1 D-arabitol-phosphate dehydrogenase 1.1.1.2 alcohol dehydrogenase (NADP+) 1.1.1.B3 (S)-specific secondary alcohol dehydrogenase 1.1.1.3 homoserine dehydrogenase 1.1.1.B4 (R)-specific secondary alcohol dehydrogenase 1.1.1.4 (R,R)-butanediol dehydrogenase 1.1.1.5 acetoin dehydrogenase 1.1.1.B5 NADP-retinol dehydrogenase 1.1.1.6 glycerol dehydrogenase 1.1.1.7 propanediol-phosphate dehydrogenase 1.1.1.8 glycerol-3-phosphate dehydrogenase (NAD+) 1.1.1.9 D-xylulose reductase 1.1.1.10 L-xylulose reductase 1.1.1.11 D-arabinitol 4-dehydrogenase 1.1.1.12 L-arabinitol 4-dehydrogenase 1.1.1.13 L-arabinitol 2-dehydrogenase 1.1.1.14 L-iditol 2-dehydrogenase 1.1.1.15 D-iditol 2-dehydrogenase 1.1.1.16 galactitol 2-dehydrogenase 1.1.1.17 mannitol-1-phosphate 5-dehydrogenase 1.1.1.18 inositol 2-dehydrogenase 1.1.1.19 glucuronate reductase 1.1.1.20 glucuronolactone reductase 1.1.1.21 aldehyde reductase 1.1.1.22 UDP-glucose 6-dehydrogenase 1.1.1.23 histidinol dehydrogenase 1.1.1.24 quinate dehydrogenase 1.1.1.25 shikimate dehydrogenase 1.1.1.26 glyoxylate reductase 1.1.1.27 L-lactate dehydrogenase 1.1.1.28 D-lactate dehydrogenase 1.1.1.29 glycerate dehydrogenase 1.1.1.30 3-hydroxybutyrate dehydrogenase 1.1.1.31 3-hydroxyisobutyrate dehydrogenase 1.1.1.32 mevaldate reductase 1.1.1.33 mevaldate reductase (NADPH) 1.1.1.34 hydroxymethylglutaryl-CoA reductase (NADPH) 1.1.1.35 3-hydroxyacyl-CoA
    [Show full text]
  • Analysis of the Expression and Single-Nucleotide Variant Frequencies of the Buyrophilin-Like 2 Gene in Patients with Uveal Melanoma
    Supplementary Online Content Amaro A, Parodi F, Diedrich K, et al. Analysis of the expression and single-nucleotide variant frequencies of the buyrophilin-like 2 gene in patients with uveal melanoma. JAMA Ophthalmol. Published online August 11, 2016. doi: 10.1001/jamaophthalmol.2016.2691. eTable 1. M1- and M2-poloarization genes eTable 2. M1- and M2-polarization genes that are associated with disease-free survival of patients with uveal melanoma This supplementary material has been provided by the authors to give readers additional information about their work. © 2016 American Medical Association. All rights reserved. Downloaded From: https://jamanetwork.com/ on 09/30/2021 eTable 1. M1- and M2-poloarization genes 203308_x NM_000195 | HPS1 3257 Hs.40456 203308_x 10 GO:00070 - AI185798 Hermansky-Pudlak syndrome 1 chr10:100 1E+08 1E+08 -1.13131 6.095084 0.859709 0.14105 1.819564 205022_s NM_001085471 FOXN3 1112 Hs.43428 205022_s 14 GO:00000 - NM_0051 forkhead box N3 chr14:896 89622516 90085494 -0.83339 6.106332 1.983495 0.324826 3.850649 204226_a NM_001164380 STAU2 27067 Hs.56181 204226_a 8 GO:00068 - NM_0143 staufen, RNA binding protein, chr8:7446 74461843 74659943 -0.95841 6.106973 0.850648 0.139291 1.804766 208639_x NM_005742 | PDIA6 10130 Hs.21210 208639_x 2 GO:00064 - BC001312 protein disulfide isomerase chr2:1092 10923518 10952960 -0.37258 6.110976 1.043652 0.170783 2.061971 204295_a NA NA NA NA 204295_a NA NA NA NM_0031 NA chrNA:-1-- -1 -1 -0.94773 6.113623 0.686679 0.112319 1.613194 202609_a NM_004447 | EPS8 2059 Hs.59116 202609_a
    [Show full text]
  • Nitroreductase and Akr1c3
    X-RAY CRYSTALLOGRAPHIC STUDIES OF THERAPEUTIC ENZYMES: NITROREDUCTASE AND AKR1C3. By ANDREW LEE LOVERING A thesis submitted to The University of Birmingham For the degree of DOCTOR OF PHILOSOPHY School of Biosciences The University of Birmingham February 2003 University of Birmingham Research Archive e-theses repository This unpublished thesis/dissertation is copyright of the author and/or third parties. The intellectual property rights of the author or third parties in respect of this work are as defined by The Copyright Designs and Patents Act 1988 or as modified by any successor legislation. Any use made of information contained in this thesis/dissertation must be in accordance with that legislation and must be properly acknowledged. Further distribution or reproduction in any format is prohibited without the permission of the copyright holder. Acknowledgements A very informal part this - at last after writing countless pages of (nearly) structured work. Great thanks first to Scott, it's been a pleasure. I think I appreciate you never dumbing anything down most, although it was hard going at the start! It's been nice (in terms of each thinking you were working with the other, in actuality I was in the pub) to have a co- supervisor in Eva (Peter too), who was wonderful in sorting out my lab work. Thanks to both. I won't forget the effort or friendship. That should get me a good reference. I had a great time in collaborating with Jon and Chris, thanks also to Anna & Anya for helping whilst I worked in their lab. Last of the semi-formal thanks goes to all the technical support on data collection trips, and that at home (Rosemary, I swear I never mean to wind you up, it's just inevitable), the BIP lot too.
    [Show full text]