AR070436A1 - Estabilizacion de deshidrogenasas con coenzimas estables - Google Patents
Estabilizacion de deshidrogenasas con coenzimas establesInfo
- Publication number
- AR070436A1 AR070436A1 ARP090100571A ARP090100571A AR070436A1 AR 070436 A1 AR070436 A1 AR 070436A1 AR P090100571 A ARP090100571 A AR P090100571A AR P090100571 A ARP090100571 A AR P090100571A AR 070436 A1 AR070436 A1 AR 070436A1
- Authority
- AR
- Argentina
- Prior art keywords
- case independently
- stable
- enzyme
- stable coenzyme
- stabilization
- Prior art date
Links
Classifications
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- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N9/00—Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
- C12N9/0004—Oxidoreductases (1.)
- C12N9/0006—Oxidoreductases (1.) acting on CH-OH groups as donors (1.1)
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N9/00—Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
- C12N9/96—Stabilising an enzyme by forming an adduct or a composition; Forming enzyme conjugates
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- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N9/00—Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
- C12N9/0004—Oxidoreductases (1.)
- C12N9/0012—Oxidoreductases (1.) acting on nitrogen containing compounds as donors (1.4, 1.5, 1.6, 1.7)
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- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N9/00—Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
- C12N9/0004—Oxidoreductases (1.)
- C12N9/0012—Oxidoreductases (1.) acting on nitrogen containing compounds as donors (1.4, 1.5, 1.6, 1.7)
- C12N9/0014—Oxidoreductases (1.) acting on nitrogen containing compounds as donors (1.4, 1.5, 1.6, 1.7) acting on the CH-NH2 group of donors (1.4)
- C12N9/0016—Oxidoreductases (1.) acting on nitrogen containing compounds as donors (1.4, 1.5, 1.6, 1.7) acting on the CH-NH2 group of donors (1.4) with NAD or NADP as acceptor (1.4.1)
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- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12Q—MEASURING OR TESTING PROCESSES INVOLVING ENZYMES, NUCLEIC ACIDS OR MICROORGANISMS; COMPOSITIONS OR TEST PAPERS THEREFOR; PROCESSES OF PREPARING SUCH COMPOSITIONS; CONDITION-RESPONSIVE CONTROL IN MICROBIOLOGICAL OR ENZYMOLOGICAL PROCESSES
- C12Q1/00—Measuring or testing processes involving enzymes, nucleic acids or microorganisms; Compositions therefor; Processes of preparing such compositions
- C12Q1/26—Measuring or testing processes involving enzymes, nucleic acids or microorganisms; Compositions therefor; Processes of preparing such compositions involving oxidoreductase
- C12Q1/32—Measuring or testing processes involving enzymes, nucleic acids or microorganisms; Compositions therefor; Processes of preparing such compositions involving oxidoreductase involving dehydrogenase
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- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12Y—ENZYMES
- C12Y101/00—Oxidoreductases acting on the CH-OH group of donors (1.1)
- C12Y101/01—Oxidoreductases acting on the CH-OH group of donors (1.1) with NAD+ or NADP+ as acceptor (1.1.1)
- C12Y101/01001—Alcohol dehydrogenase (1.1.1.1)
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- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12Y—ENZYMES
- C12Y101/00—Oxidoreductases acting on the CH-OH group of donors (1.1)
- C12Y101/01—Oxidoreductases acting on the CH-OH group of donors (1.1) with NAD+ or NADP+ as acceptor (1.1.1)
- C12Y101/01006—Glycerol dehydrogenase (1.1.1.6)
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- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12Y—ENZYMES
- C12Y101/00—Oxidoreductases acting on the CH-OH group of donors (1.1)
- C12Y101/01—Oxidoreductases acting on the CH-OH group of donors (1.1) with NAD+ or NADP+ as acceptor (1.1.1)
- C12Y101/01027—L-Lactate dehydrogenase (1.1.1.27)
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- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12Y—ENZYMES
- C12Y101/00—Oxidoreductases acting on the CH-OH group of donors (1.1)
- C12Y101/01—Oxidoreductases acting on the CH-OH group of donors (1.1) with NAD+ or NADP+ as acceptor (1.1.1)
- C12Y101/01028—D-Lactate dehydrogenase (1.1.1.28)
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- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12Y—ENZYMES
- C12Y101/00—Oxidoreductases acting on the CH-OH group of donors (1.1)
- C12Y101/01—Oxidoreductases acting on the CH-OH group of donors (1.1) with NAD+ or NADP+ as acceptor (1.1.1)
- C12Y101/01037—Malate dehydrogenase (1.1.1.37)
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- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12Y—ENZYMES
- C12Y101/00—Oxidoreductases acting on the CH-OH group of donors (1.1)
- C12Y101/01—Oxidoreductases acting on the CH-OH group of donors (1.1) with NAD+ or NADP+ as acceptor (1.1.1)
- C12Y101/01047—Glucose 1-dehydrogenase (1.1.1.47)
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- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12Y—ENZYMES
- C12Y104/00—Oxidoreductases acting on the CH-NH2 group of donors (1.4)
- C12Y104/01—Oxidoreductases acting on the CH-NH2 group of donors (1.4) with NAD+ or NADP+ as acceptor (1.4.1)
- C12Y104/01005—L-Amino-acid dehydrogenase (1.4.1.5)
Landscapes
- Chemical & Material Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Health & Medical Sciences (AREA)
- Organic Chemistry (AREA)
- Engineering & Computer Science (AREA)
- Wood Science & Technology (AREA)
- Zoology (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Genetics & Genomics (AREA)
- General Engineering & Computer Science (AREA)
- General Health & Medical Sciences (AREA)
- Biochemistry (AREA)
- Biotechnology (AREA)
- Molecular Biology (AREA)
- Microbiology (AREA)
- Medicinal Chemistry (AREA)
- Biomedical Technology (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Physics & Mathematics (AREA)
- Analytical Chemistry (AREA)
- Biophysics (AREA)
- Immunology (AREA)
- Measuring Or Testing Involving Enzymes Or Micro-Organisms (AREA)
- Enzymes And Modification Thereof (AREA)
Abstract
Procedimiento para la estabilizacion de una enzima deshidrogenasa por almacenamiento de la enzima en presencia de una coenzima estable. Además una enzima estabilizada con una coenzima estable así como también a su uso en elementos de prueba para la determinacion de substancias a analizar. Reivindicacion 5: Procedimiento de acuerdo con una de las reivindicaciones 1 a 4, caracterizado porque la coenzima estable es seleccionada entre compuestos de nicotinamida-adenina-dinucleotido (NAD/NADH) y nicotinamida-adenina-dinucleotido fosfato (NADP/NADPH) estables y el compuesto de la Formula (1). Reivindicacion 6: Procedimiento de acuerdo con la reivindicacion 5, caracterizado porque la coenzima estable es seleccionada entre los compuestos con la formula general (2), con: A = adenina o un análogo de la misma, T = en cada caso independientemente O, S; U = en cada caso independientemente OH, SH, BH3-, BCNH2-; V = en cada caso independientemente OH o un grupo fosfato, o dos grupos que forman un grupo fosfato cíclico; W = COOR, CON(R)2, COR, CSN(R)2 con R = en cada caso independientemente H o alquilo C1-2; X1, X2 = en cada caso independientemente O, CH2, CHCH3, C(CH3)2, NH, NCH3; Y = NH, S, O, CH2; Z = es un resto orgánico lineal o cíclico, con la condicion de que Z y el resto piridina no estén unidos por una union glicosídica, o una sal o eventualmente una forma reducida del mismo.
Applications Claiming Priority (1)
Application Number | Priority Date | Filing Date | Title |
---|---|---|---|
EP08003054A EP2093284A1 (de) | 2008-02-19 | 2008-02-19 | Stabilisierung von Dehydrogenasen mit stabilen Coenzymen |
Publications (1)
Publication Number | Publication Date |
---|---|
AR070436A1 true AR070436A1 (es) | 2010-04-07 |
Family
ID=39768713
Family Applications (1)
Application Number | Title | Priority Date | Filing Date |
---|---|---|---|
ARP090100571A AR070436A1 (es) | 2008-02-19 | 2009-02-19 | Estabilizacion de deshidrogenasas con coenzimas estables |
Country Status (15)
Country | Link |
---|---|
US (2) | US9896666B2 (es) |
EP (2) | EP2093284A1 (es) |
JP (2) | JP5758128B2 (es) |
KR (3) | KR20120134142A (es) |
CN (3) | CN101945999B (es) |
AR (1) | AR070436A1 (es) |
AU (1) | AU2009216908B9 (es) |
BR (1) | BRPI0907839A2 (es) |
CA (1) | CA2721718C (es) |
HK (1) | HK1208703A1 (es) |
MX (1) | MX2010008920A (es) |
RU (1) | RU2499834C2 (es) |
TW (1) | TWI482860B (es) |
WO (1) | WO2009103540A1 (es) |
ZA (1) | ZA201006638B (es) |
Families Citing this family (27)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
JP4786451B2 (ja) * | 2005-07-28 | 2011-10-05 | エフ ホフマン−ラ ロッシュ アクチェン ゲゼルシャフト | Nad/nadhの安定化 |
WO2010094632A1 (de) * | 2009-02-19 | 2010-08-26 | F. Hoffmann-La Roche Ag | Schnelle reaktionskinetik von enzymen mit niedriger aktivität in trockenen chemieschichten |
EP2093284A1 (de) | 2008-02-19 | 2009-08-26 | F.Hoffmann-La Roche Ag | Stabilisierung von Dehydrogenasen mit stabilen Coenzymen |
EP2398909B1 (de) | 2009-02-19 | 2015-07-22 | F. Hoffmann-La Roche AG | Schnelle reaktionskinetik von enzymen mit niedriger aktivität in trockenen chemieschichten |
EP2226007A1 (de) | 2009-02-19 | 2010-09-08 | Roche Diagnostics GmbH | Testelementmagazin mit abgedeckten Testfeldern |
EP2226008A1 (de) | 2009-02-19 | 2010-09-08 | Roche Diagnostics GmbH | Verfahren zur Herstellung eines analytischen Magazins |
CN102325496B (zh) | 2009-02-19 | 2015-10-07 | 霍夫曼-拉罗奇有限公司 | 分析辅助工具的节省空间的储存 |
EP2292751A1 (de) * | 2009-08-20 | 2011-03-09 | Roche Diagnostics GmbH | Stabilisierung von Enzymen mit stabilen Coenzymen |
CA2782943C (en) * | 2009-12-16 | 2014-09-09 | F. Hoffmann-La Roche Ag | Detecting the decomposition of enzymes in a test element by means of controlled release of a protected analyte |
EP2636750A1 (en) * | 2012-03-06 | 2013-09-11 | Roche Diagniostics GmbH | Compatible solute ectoine as well as derivatives thereof for enzyme stabilization |
PL2864765T3 (pl) | 2012-06-22 | 2021-10-11 | F.Hoffmann-La Roche Ag | Sposób i urządzenie do wykrywania analitu w płynie ustrojowym |
US8920628B2 (en) | 2012-11-02 | 2014-12-30 | Roche Diagnostics Operations, Inc. | Systems and methods for multiple analyte analysis |
US8921061B2 (en) | 2012-11-02 | 2014-12-30 | Roche Diagnostics Operations, Inc. | Reagent materials and associated test elements |
WO2014096184A1 (en) | 2012-12-20 | 2014-06-26 | Roche Diagnostics Gmbh | Method for analyzing a sample of a body fluid |
PL2936124T3 (pl) | 2012-12-20 | 2017-08-31 | F.Hoffmann-La Roche Ag | Sposoby oceniania medycznych krzywych pomiarowych |
EP2781919A1 (en) | 2013-03-19 | 2014-09-24 | Roche Diagniostics GmbH | Method / device for generating a corrected value of an analyte concentration in a sample of a body fluid |
EP2994536B1 (en) | 2013-05-08 | 2017-06-14 | Roche Diabetes Care GmbH | Stabilization of enzymes by nicotinic acid |
CN105247069A (zh) * | 2013-06-04 | 2016-01-13 | 豪夫迈·罗氏有限公司 | 用于fret的新化合物及与其相关的方法 |
EP3063169B1 (en) | 2013-10-29 | 2018-10-10 | F. Hoffmann-La Roche AG | Nano-enzyme containers for test elements |
EP3074524B1 (en) | 2013-11-27 | 2019-11-06 | Roche Diabetes Care GmbH | Composition comprising up-converting phosphors for detecting an analyte |
EP2927319A1 (en) | 2014-03-31 | 2015-10-07 | Roche Diagnostics GmbH | High load enzyme immobilization by crosslinking |
KR101896820B1 (ko) | 2014-04-14 | 2018-09-07 | 에프. 호프만-라 로슈 아게 | 페나지늄 매개체 |
EP3183246B1 (en) | 2014-08-22 | 2020-09-23 | Roche Diagnostics GmbH | Redoxindicators |
CN107779459B (zh) * | 2016-08-31 | 2021-06-08 | 安琪酵母股份有限公司 | 葡萄糖脱氢酶dna分子、载体和菌株及应用 |
EP3523639A4 (en) | 2016-10-05 | 2020-06-03 | H. Hoffnabb-La Roche Ag | DETECTION REAGENTS AND ELECTRODE ARRANGEMENTS FOR DIAGNOSTIC MULTIANALYTE TEST ELEMENTS AND METHOD FOR USE THEREOF |
EP3339431A1 (en) | 2016-12-22 | 2018-06-27 | Roche Diabetes Care GmbH | Glucose dehydrogenase variants with improved properties |
EP3759231B1 (en) | 2018-02-28 | 2023-10-18 | F. Hoffmann-La Roche AG | Biocompatibility coating for continuous analyte measurement |
Family Cites Families (16)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
SU1043568A1 (ru) * | 1981-06-11 | 1983-09-23 | Московский Ордена Ленина,Ордена Октябрьской Революции И Ордена Трудового Красного Знамени Государственный Университет Им.М.В.Ломоносова | Способ определени активности дегидрогеназ крови |
DE19543493A1 (de) * | 1995-11-22 | 1997-05-28 | Boehringer Mannheim Gmbh | Stabilisierte Coenzym-Lösungen und deren Verwendung zur Bestimmung von Dehydrogenasen bzw. deren Substrate im alkalischen Milieu |
US5801006A (en) | 1997-02-04 | 1998-09-01 | Specialty Assays, Inc. | Use of NADPH and NADH analogs in the measurement of enzyme activities and metabolites |
US6380380B1 (en) | 1999-01-04 | 2002-04-30 | Specialty Assays, Inc. | Use of nicotinamide adenine dinucleotide (NAD) and nicotinamide adenine dinucliotide phosphate (NADP) analogs to measure enzyme activities metabolites and substrates |
AU2001262702A1 (en) | 2000-06-07 | 2001-12-17 | Asahi Kasei Kabushiki Kaisha | Coenzyme derivatives and enzymes appropriate therefor |
AU1099102A (en) * | 2000-10-31 | 2002-05-15 | Koji Sode | Novel glucose dehydrogenase and process for producing the dehydrogenase |
JP2003310274A (ja) * | 2002-04-30 | 2003-11-05 | Amano Enzyme Inc | グルコース脱水素酵素およびそれをコードする遺伝子 |
AU2003240260B2 (en) | 2002-05-16 | 2008-05-22 | F. Hoffmann-La Roche Ag | Method and reagent system having a non-regenerative enzyme-coenzyme complex |
EP1660648B1 (en) * | 2003-08-11 | 2013-10-09 | Codexis, Inc. | Improved glucose dehydrogenase polypeptides and related polynucleotides |
AU2005220022B2 (en) | 2004-03-06 | 2010-10-07 | F. Hoffmann-La Roche Ag | Body fluid sampling device |
US7172890B2 (en) * | 2004-10-28 | 2007-02-06 | Roche Diagnostics Gmbh | Inactivated enzyme variants and associated process and reagent system |
JP4786451B2 (ja) | 2005-07-28 | 2011-10-05 | エフ ホフマン−ラ ロッシュ アクチェン ゲゼルシャフト | Nad/nadhの安定化 |
DE102005035461A1 (de) | 2005-07-28 | 2007-02-15 | Roche Diagnostics Gmbh | Stabile NAD/NADH-Derivate |
EP2093284A1 (de) * | 2008-02-19 | 2009-08-26 | F.Hoffmann-La Roche Ag | Stabilisierung von Dehydrogenasen mit stabilen Coenzymen |
WO2010009432A1 (en) | 2008-07-17 | 2010-01-21 | Horizon Therapeutics, Inc. | Nsaid dose unit formulations with h2-receptor antagonists and methods of use |
EP2398909B1 (de) | 2009-02-19 | 2015-07-22 | F. Hoffmann-La Roche AG | Schnelle reaktionskinetik von enzymen mit niedriger aktivität in trockenen chemieschichten |
-
2008
- 2008-02-19 EP EP08003054A patent/EP2093284A1/de not_active Ceased
-
2009
- 2009-02-18 TW TW098105120A patent/TWI482860B/zh active
- 2009-02-19 JP JP2010547110A patent/JP5758128B2/ja not_active Expired - Fee Related
- 2009-02-19 KR KR1020127027270A patent/KR20120134142A/ko not_active Application Discontinuation
- 2009-02-19 CN CN200980105640.6A patent/CN101945999B/zh not_active Expired - Fee Related
- 2009-02-19 CN CN201410680334.8A patent/CN104450659A/zh active Pending
- 2009-02-19 KR KR1020107020894A patent/KR101381004B1/ko active IP Right Grant
- 2009-02-19 CA CA2721718A patent/CA2721718C/en not_active Expired - Fee Related
- 2009-02-19 WO PCT/EP2009/001206 patent/WO2009103540A1/de active Application Filing
- 2009-02-19 RU RU2010138610/10A patent/RU2499834C2/ru not_active IP Right Cessation
- 2009-02-19 EP EP09712033.1A patent/EP2245152B1/de active Active
- 2009-02-19 BR BRPI0907839-8A patent/BRPI0907839A2/pt not_active Application Discontinuation
- 2009-02-19 AU AU2009216908A patent/AU2009216908B9/en not_active Revoked
- 2009-02-19 MX MX2010008920A patent/MX2010008920A/es active IP Right Grant
- 2009-02-19 AR ARP090100571A patent/AR070436A1/es not_active Application Discontinuation
- 2009-02-19 KR KR1020137013118A patent/KR20130081300A/ko not_active Application Discontinuation
-
2010
- 2010-02-12 CN CN2010800085457A patent/CN102325896A/zh active Pending
- 2010-02-12 JP JP2011550531A patent/JP6113405B2/ja not_active Expired - Fee Related
- 2010-08-19 US US12/859,654 patent/US9896666B2/en active Active
- 2010-09-16 ZA ZA2010/06638A patent/ZA201006638B/en unknown
-
2015
- 2015-09-23 HK HK15109305.4A patent/HK1208703A1/xx unknown
-
2018
- 2018-01-11 US US15/868,055 patent/US11220674B2/en active Active
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