Development Perspective of Bioelectrocatalysis-Based Biosensors
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Itraq-Based Quantitative Proteomics Analysis Reveals the Mechanism Underlying the Weakening of Carbon Metabolism in Chlorotic Tea Leaves
Article iTRAQ-Based Quantitative Proteomics Analysis Reveals the Mechanism Underlying the Weakening of Carbon Metabolism in Chlorotic Tea Leaves Fang Dong 1,2, Yuanzhi Shi 1,2, Meiya Liu 1,2, Kai Fan 1,2, Qunfeng Zhang 1,2,* and Jianyun Ruan 1,2 1 Tea Research Institute, Chinese Academy of Agricultural Sciences, Hangzhou 310008, China; [email protected] (F.D.); [email protected] (Y.S.); [email protected] (M.L.); [email protected] (K.F.); [email protected] (J.R.) 2 Key Laboratory for Plant Biology and Resource Application of Tea, the Ministry of Agriculture, Hangzhou 310008, China * Correspondence: [email protected]; Tel.: +86-571-8527-0665 Received: 7 November 2018; Accepted: 5 December 2018; Published: 7 December 2018 Abstract: To uncover mechanism of highly weakened carbon metabolism in chlorotic tea (Camellia sinensis) plants, iTRAQ (isobaric tags for relative and absolute quantification)-based proteomic analyses were employed to study the differences in protein expression profiles in chlorophyll-deficient and normal green leaves in the tea plant cultivar “Huangjinya”. A total of 2110 proteins were identified in “Huangjinya”, and 173 proteins showed differential accumulations between the chlorotic and normal green leaves. Of these, 19 proteins were correlated with RNA expression levels, based on integrated analyses of the transcriptome and proteome. Moreover, the results of our analysis of differentially expressed proteins suggested that primary carbon metabolism (i.e., carbohydrate synthesis and transport) was inhibited in chlorotic tea leaves. The differentially expressed genes and proteins combined with photosynthetic phenotypic data indicated that 4-coumarate-CoA ligase (4CL) showed a major effect on repressing flavonoid metabolism, and abnormal developmental chloroplast inhibited the accumulation of chlorophyll and flavonoids because few carbon skeletons were provided as a result of a weakened primary carbon metabolism. -
Deletion of the Gene Encoding the Reductase Component of 3
Yeh et al. Microbial Cell Factories 2014, 13:130 http://www.microbialcellfactories.com/content/13/1/130 RESEARCH Open Access Deletion of the gene encoding the reductase component of 3-ketosteroid 9α-hydroxylase in Rhodococcus equi USA-18 disrupts sterol catabolism, leading to the accumulation of 3-oxo-23,24-bisnorchola-1,4-dien-22-oic acid and 1,4-androstadiene-3,17-dione Chin-Hsing Yeh1, Yung-Shun Kuo1, Che-Ming Chang1, Wen-Hsiung Liu2, Meei-Ling Sheu3 and Menghsiao Meng1* Abstract The gene encoding the putative reductase component (KshB) of 3-ketosteroid 9α-hydroxylase was cloned from Rhodococcus equi USA-18, a cholesterol oxidase-producing strain formerly named Arthrobacter simplex USA-18, by PCR according to consensus amino acid motifs of several bacterial KshB subunits. Deletion of the gene in R. equi USA-18 by a PCR-targeted gene disruption method resulted in a mutant strain that could accumulate up to 0.58 mg/ml 1,4-androstadiene-3,17-dione (ADD) in the culture medium when 0.2% cholesterol was used as the carbon source, indicating the involvement of the deleted enzyme in 9α-hydroxylation of steroids. In addition, this mutant also accumulated 3-oxo-23,24-bisnorchola-1,4-dien-22-oic acid (Δ1,4-BNC). Because both ADD and Δ1,4-BNC are important intermediates for the synthesis of steroid drugs, this mutant derived from R. equi USA-18 may deserve further investigation for its application potential. Background generally believed to be carried out by cholesterol oxidase, Steroid drugs, including androgens, anabolic steroids, es- which catalyzes the oxidation of the 3β-hydroxyl moiety of trogens and corticosteroids, have been widely used for a sterols with the simultaneous isomerization of Δ5 to Δ4, variety of health purposes. -
Engineering the Substrate Specificity of Galactose Oxidase
Engineering the Substrate Specificity of Galactose Oxidase Lucy Ann Chappell BSc. (Hons) Submitted in accordance with the requirements for the degree of Doctor of Philosophy The University of Leeds School of Molecular and Cellular Biology September 2013 The candidate confirms that the work submitted is her own and that appropriate credit has been given where reference has been made to the work of others. This copy has been supplied on the understanding that it is copyright material and that no quotation from the thesis may be published without proper acknowledgement © 2013 The University of Leeds and Lucy Ann Chappell The right of Lucy Ann Chappell to be identified as Author of this work has been asserted by her in accordance with the Copyright, Designs and Patents Act 1988. ii Acknowledgements My greatest thanks go to Prof. Michael McPherson for the support, patience, expertise and time he has given me throughout my PhD. Many thanks to Dr Bruce Turnbull for always finding time to help me with the Chemistry side of the project, particularly the NMR work. Also thanks to Dr Arwen Pearson for her support, especially reading and correcting my final thesis. Completion of the laboratory work would not have been possible without the help of numerous lab members and friends who have taught me so much, helped develop my scientific skills and provided much needed emotional support – thank you for your patience and friendship: Dr Thembi Gaule, Dr Sarah Deacon, Dr Christian Tiede, Dr Saskia Bakker, Ms Briony Yorke and Mrs Janice Robottom. Thank you to three students I supervised during my PhD for their friendship and contributions to the project: Mr Ciaran Doherty, Ms Lito Paraskevopoulou and Ms Upasana Mandal. -
Current IUBMB Recommendations on Enzyme Nomenclature and Kinetics$
Perspectives in Science (2014) 1,74–87 Available online at www.sciencedirect.com www.elsevier.com/locate/pisc REVIEW Current IUBMB recommendations on enzyme nomenclature and kinetics$ Athel Cornish-Bowden CNRS-BIP, 31 chemin Joseph-Aiguier, B.P. 71, 13402 Marseille Cedex 20, France Received 9 July 2013; accepted 6 November 2013; Available online 27 March 2014 KEYWORDS Abstract Enzyme kinetics; The International Union of Biochemistry (IUB, now IUBMB) prepared recommendations for Rate of reaction; describing the kinetic behaviour of enzymes in 1981. Despite the more than 30 years that have Enzyme passed since these have not subsequently been revised, though in various respects they do not nomenclature; adequately cover current needs. The IUBMB is also responsible for recommendations on the Enzyme classification naming and classification of enzymes. In contrast to the case of kinetics, these recommenda- tions are kept continuously up to date. & 2014 The Author. Published by Elsevier GmbH. This is an open access article under the CC BY license (http://creativecommons.org/licenses/by/3.0/). Contents Introduction...................................................................75 Kinetics introduction...........................................................75 Introduction to enzyme nomenclature ................................................76 Basic definitions ................................................................76 Rates of consumption and formation .................................................76 Rate of reaction .............................................................76 -
Production of 4-Ene-3-Ketosteroids in Corynebacterium Glutamicum
catalysts Article Production of 4-Ene-3-ketosteroids in Corynebacterium glutamicum Julia García-Fernández 1, Beatriz Galán 1, Carmen Felpeto-Santero 1, José L. Barredo 2 and José L. García 1,* 1 Department of Environmental Biotechnology, Centro de Investigaciones Biológicas (CSIC), Ramiro de Maeztu 9, 28040 Madrid, Spain; [email protected] (J.G.-F.); [email protected] (B.G.); [email protected] (C.F.-S.) 2 Department of Biotechnology, Crystal Pharma, A Division of Albany Molecular Research Inc. (AMRI), 47151 Boecillo Valladolid, Spain; [email protected] * Correspondence: [email protected]; Tel.: +34-918-373-112 Received: 29 September 2017; Accepted: 20 October 2017; Published: 27 October 2017 Abstract: Corynebacterium glutamicum has been widely used for the industrial production of amino acids and many value-added chemicals; however, it has not been exploited for the production of steroids. Using C. glutamicum as a cellular biocatalyst we have expressed the 3β-hydroxysteroid dehydrogenase/isomerase MSMEG_5228 from Mycobacterium smegmatis to demonstrate that the resulting recombinant strain is able to oxidize in vivo C19 and C21 3-OH-steroids to their corresponding keto-derivatives. This new approach constitutes a proof of concept of a biotechnological process for producing value-added intermediates such as 4-pregnen-16α,17α-epoxy-16β-methyl-3,20-dione. Keywords: 3-OH-steroids; biotransformation; dehydrogenase; Rhodococcus and Corynebacterium expression systems 1. Introduction Corynebacterium glutamicum has been widely used for the industrial production of amino acids, but the publication of its complete genome [1,2] has provided the basis for an enormous progress in the use of this microorganism for other biotechnological applications placing it as an ideal chassis within the top ranking of cell factories [3]. -
Generated by SRI International Pathway Tools Version 25.0, Authors S
Authors: Pallavi Subhraveti Ron Caspi Quang Ong Peter D Karp An online version of this diagram is available at BioCyc.org. Biosynthetic pathways are positioned in the left of the cytoplasm, degradative pathways on the right, and reactions not assigned to any pathway are in the far right of the cytoplasm. Transporters and membrane proteins are shown on the membrane. Ingrid Keseler Periplasmic (where appropriate) and extracellular reactions and proteins may also be shown. Pathways are colored according to their cellular function. Gcf_000725805Cyc: Streptomyces xanthophaeus Cellular Overview Connections between pathways are omitted for legibility. -
Collection of Information on Enzymes a Great Deal of Additional Information on the European Union Is Available on the Internet
European Commission Collection of information on enzymes A great deal of additional information on the European Union is available on the Internet. It can be accessed through the Europa server (http://europa.eu.int). Luxembourg: Office for Official Publications of the European Communities, 2002 ISBN 92-894-4218-2 © European Communities, 2002 Reproduction is authorised provided the source is acknowledged. Final Report „Collection of Information on Enzymes“ Contract No B4-3040/2000/278245/MAR/E2 in co-operation between the Federal Environment Agency Austria Spittelauer Lände 5, A-1090 Vienna, http://www.ubavie.gv.at and the Inter-University Research Center for Technology, Work and Culture (IFF/IFZ) Schlögelgasse 2, A-8010 Graz, http://www.ifz.tu-graz.ac.at PROJECT TEAM (VIENNA / GRAZ) Werner Aberer c Maria Hahn a Manfred Klade b Uli Seebacher b Armin Spök (Co-ordinator Graz) b Karoline Wallner a Helmut Witzani (Co-ordinator Vienna) a a Austrian Federal Environmental Agency (UBA), Vienna b Inter-University Research Center for Technology, Work, and Culture - IFF/IFZ, Graz c University of Graz, Department of Dermatology, Division of Environmental Dermatology, Graz Executive Summary 5 EXECUTIVE SUMMARY Technical Aspects of Enzymes (Chapter 3) Application of enzymes (Section 3.2) Enzymes are applied in various areas of application, the most important ones are technical use, manufacturing of food and feedstuff, cosmetics, medicinal products and as tools for re- search and development. Enzymatic processes - usually carried out under mild conditions - are often replacing steps in traditional chemical processes which were carried out under harsh industrial environments (temperature, pressures, pH, chemicals). Technical enzymes are applied in detergents, for pulp and paper applications, in textile manufacturing, leather industry, for fuel production and for the production of pharmaceuticals and chiral substances in the chemical industry. -
Insight V-CHEM General Health Profile
【Product Name】 General Health Profile 【Packing Specification】 1 Disc / Sample 【Instrument】 See the InSight V-CHEM chemistry analyser Operator’s Manual for complete information on use of the analyser. 【Intended Use】 The General Health Profile used with the InSight V-CHEM chemistry analyser is intended to be used for the in vitro quantitative determination of total Protein (TP), albumin (ALB), total bilirubin (TBIL), alanine aminotransferase (ALT), blood urea (BUN), creatinine (CRE), amylase (AMY), creatinekinase (CK), calcium (Ca2+), phosphorus (P), alkaline Phosphatase (ALP), glucose (GLU), and total cholesterol (CHOL)in heparinised whole blood, heparinised plasma, or serum in a clinical laboratory setting or point of care location. The General Health Profile and the InSight V-CHEM chemistry analyser comprise an in vitro diagnostic system that aids the physician in the following disorders: liver and gall bladder diseases, urinary system diseases, carbohydrate metabolism disorders, lipid metabolism disorders, cardiovascular disease and pancreatic diseases. 【Test Principles】 This product, which is based on spectrophotometry, is used to quantitatively determine the concentration or activity of the 13 biochemical indicators in the sample. The test principles are as follows: (1) Total Protein (TP) The total protein method is a Biuret reaction, the protein solution is treated with cupric [Cu(II)] ions in a strong alkaline medium. The Cu(II) ions react with peptide bonds between the carbonyl oxygen and amide nitrogen atoms to form a coloured Cu-protein complex. The amount of total protein present in the sample is directly proportional to the absorbance of the Cu-protein complex. The total protein test is an endpoint reaction and the absorbance is measured as the difference in absorbance between 550 nm and 800 nm. -
Western Blot Sandwich ELISA Immunohistochemistry
$$ 250 - 150 - 100 - 75 - 50 - 37 - Western Blot 25 - 20 - 15 - 10 - 1.4 1.2 1 0.8 0.6 OD 450 0.4 Sandwich ELISA 0.2 0 0.01 0.1 1 10 100 1000 Recombinant Protein Concentration(mg/ml) Immunohistochemistry Immunofluorescence 1 2 3 250 - 150 - 100 - 75 - 50 - Immunoprecipitation 37 - 25 - 20 - 15 - 100 80 60 % of Max 40 Flow Cytometry 20 0 3 4 5 0 102 10 10 10 www.abnova.com June 2013 (Fourth Edition) 37 38 53 Cat. Num. Product Name Cat. Num. Product Name MAB5411 A1/A2 monoclonal antibody, clone Z2A MAB3882 Adenovirus type 6 monoclonal antibody, clone 143 MAB0794 A1BG monoclonal antibody, clone 54B12 H00000126-D01 ADH1C MaxPab rabbit polyclonal antibody (D01) H00000002-D01 A2M MaxPab rabbit polyclonal antibody (D01) H00000127-D01 ADH4 MaxPab rabbit polyclonal antibody (D01) MAB0759 A2M monoclonal antibody, clone 3D1 H00000131-D01 ADH7 MaxPab rabbit polyclonal antibody (D01) MAB0758 A2M monoclonal antibody, clone 9A3 PAB0005 ADIPOQ polyclonal antibody H00051166-D01 AADAT MaxPab rabbit polyclonal antibody (D01) PAB0006 Adipoq polyclonal antibody H00000016-D01 AARS MaxPab rabbit polyclonal antibody (D01) PAB5030 ADIPOQ polyclonal antibody MAB8772 ABCA1 monoclonal antibody, clone AB.H10 PAB5031 ADIPOQ polyclonal antibody MAB8291 ABCA1 monoclonal antibody, clone AB1.G6 PAB5069 Adipoq polyclonal antibody MAB3345 ABCB1 monoclonal antibody, clone MRK16 PAB5070 Adipoq polyclonal antibody MAB3389 ABCC1 monoclonal antibody, clone QCRL-2 PAB5124 Adipoq polyclonal antibody MAB5157 ABCC1 monoclonal antibody, clone QCRL-3 PAB9125 ADIPOQ polyclonal antibody -
( 12 ) United States Patent
US010195209B2 (12 ) United States Patent ( 10 ) Patent No. : US 10 , 195 ,209 B2 Gish et al. (45 ) Date of Patent: * Feb . 5 , 2019 (54 ) ANTI- HULRRC15 ANTIBODY DRUG 4 ,634 ,665 A 1 / 1987 Axel 4 ,716 , 111 A 12 / 1987 Osband CONJUGATES AND METHODS FOR THEIR 4 ,737 , 456 A 4 / 1988 Weng USE 4 , 816 ,397 A 3 / 1989 Boss 4 , 816 ,457 A 3 / 1989 Baldwin (71 ) Applicants :AbbVie Inc. , North Chicago , IL (US ) ; 4 , 968 ,615 A 11 / 1990 Koszinowski AbbVie Biotherapeutics Inc. , 5 , 168 , 062 A 12 / 1992 Stinski 5 , 179 ,017 A 1 / 1993 Axel Redwood City , CA (US ) 5 , 225 , 539 A 7 / 1993 Winter 5 , 413 , 923 A 5 / 1995 Kucherlapati ( 72 ) Inventors : Kurt C . Gish , Piedmont, CA (US ) ; 5 ,530 , 101 A 6 /1996 Queen Jonathan A . Hickson , Lake Villa , IL 5 , 545 , 806 A 8 / 1996 Lonberg (US ) ; Susan Elizabeth Morgan - Lappe , 5 , 565 ,332 A 10 / 1996 Hoogenboom Riverwoods, IL (US ) ; James W . 5 , 569 , 825 A 10 / 1996 Lonberg 5 ,585 ,089 A 12 / 1996 Queen Purcell, San Francisco , CA (US ) 5 ,625 , 126 A 4 / 1997 Lonberg 5 ,633 , 425 A 5 / 1997 Lonberg ( 73 ) Assignees: AbbVie Inc. , North Chicago , IL (US ) ; 5 ,658 , 570 A 8 / 1997 Newman AbbVie Biotherapeutics Inc . , 5 ,661 ,016 A 8 / 1997 Lonberg Redwood City , CA (US ) 5 ,681 , 722 A 10 / 1997 Newman 5 ,693 , 761 A 12 / 1997 Queen 5 ,693 , 762 A 12 / 1997 Queen ( * ) Notice : Subject to any disclaimer, the term of this 5 ,693 , 780 A 12 / 1997 Newman patent is extended or adjusted under 35 5 , 807 ,715 A 9 / 1998 Morrison U . -
WO 2012/170711 Al 13 December 2012 (13.12.2012) P O P C T
(12) INTERNATIONAL APPLICATION PUBLISHED UNDER THE PATENT COOPERATION TREATY (PCT) (19) World Intellectual Property Organization International Bureau (10) International Publication Number (43) International Publication Date WO 2012/170711 Al 13 December 2012 (13.12.2012) P O P C T (51) International Patent Classification: (72) Inventors; and G01N33/5 74 (2006.01) (75) Inventors/Applicants (for US only): PAWLOWSKI, Traci [US/US]; 2014 N Milkweed Loop, Phoenix, AZ (21) International Application Number: 85037 (US). YEATTS, Kimberly [US/US]; 109 E. Pierce PCT/US2012/041387 Street, Tempe, AZ 85281 (US). AKHAVAN, Ray (22) International Filing Date: [US/US]; 5804 Malvern Hill Ct, Haymarket, VA 201 69 7 June 2012 (07.06.2012) (US). (25) Filing Language: English (74) Agent: AKHAVAN, Ramin; Caris Science, Inc., 6655 N. MacArthur Blvd., Irving, TX 75039 (US). (26) Publication Language: English (81) Designated States (unless otherwise indicated, for every (30) Priority Data: kind of national protection available): AE, AG, AL, AM, 61/494,196 7 June 201 1 (07.06.201 1) AO, AT, AU, AZ, BA, BB, BG, BH, BR, BW, BY, BZ, 61/494,355 7 June 201 1 (07.06.201 1) CA, CH, CL, CN, CO, CR, CU, CZ, DE, DK, DM, DO, 61/507,989 14 July 201 1 (14.07.201 1) DZ, EC, EE, EG, ES, FI, GB, GD, GE, GH, GM, GT, HN, (71) Applicant (for all designated States except US): CARIS HR, HU, ID, IL, IN, IS, JP, KE, KG, KM, KN, KP, KR, LIFE SCIENCES LUXEMBOURG HOLDINGS, KZ, LA, LC, LK, LR, LS, LT, LU, LY, MA, MD, ME, S.A.R.L [LU/LU]; Rue De Maraichers, L2124 Luxem MG, MK, MN, MW, MX, MY, MZ, NA, NG, NI, NO, NZ, bourg, Grand-Duche De Luxembourg (LU). -
WO 2012/174282 A2 20 December 2012 (20.12.2012) P O P C T
(12) INTERNATIONAL APPLICATION PUBLISHED UNDER THE PATENT COOPERATION TREATY (PCT) (19) World Intellectual Property Organization International Bureau (10) International Publication Number (43) International Publication Date WO 2012/174282 A2 20 December 2012 (20.12.2012) P O P C T (51) International Patent Classification: David [US/US]; 13539 N . 95th Way, Scottsdale, AZ C12Q 1/68 (2006.01) 85260 (US). (21) International Application Number: (74) Agent: AKHAVAN, Ramin; Caris Science, Inc., 6655 N . PCT/US20 12/0425 19 Macarthur Blvd., Irving, TX 75039 (US). (22) International Filing Date: (81) Designated States (unless otherwise indicated, for every 14 June 2012 (14.06.2012) kind of national protection available): AE, AG, AL, AM, AO, AT, AU, AZ, BA, BB, BG, BH, BR, BW, BY, BZ, English (25) Filing Language: CA, CH, CL, CN, CO, CR, CU, CZ, DE, DK, DM, DO, Publication Language: English DZ, EC, EE, EG, ES, FI, GB, GD, GE, GH, GM, GT, HN, HR, HU, ID, IL, IN, IS, JP, KE, KG, KM, KN, KP, KR, (30) Priority Data: KZ, LA, LC, LK, LR, LS, LT, LU, LY, MA, MD, ME, 61/497,895 16 June 201 1 (16.06.201 1) US MG, MK, MN, MW, MX, MY, MZ, NA, NG, NI, NO, NZ, 61/499,138 20 June 201 1 (20.06.201 1) US OM, PE, PG, PH, PL, PT, QA, RO, RS, RU, RW, SC, SD, 61/501,680 27 June 201 1 (27.06.201 1) u s SE, SG, SK, SL, SM, ST, SV, SY, TH, TJ, TM, TN, TR, 61/506,019 8 July 201 1(08.07.201 1) u s TT, TZ, UA, UG, US, UZ, VC, VN, ZA, ZM, ZW.