JP5851401B2 - 安定な補酵素による酵素の安定化 - Google Patents
安定な補酵素による酵素の安定化 Download PDFInfo
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- JP5851401B2 JP5851401B2 JP2012525165A JP2012525165A JP5851401B2 JP 5851401 B2 JP5851401 B2 JP 5851401B2 JP 2012525165 A JP2012525165 A JP 2012525165A JP 2012525165 A JP2012525165 A JP 2012525165A JP 5851401 B2 JP5851401 B2 JP 5851401B2
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| PCT/EP2010/062045 WO2011020856A1 (de) | 2009-08-20 | 2010-08-18 | Stabilisierung von enzymen mit stabilen coenzymen |
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| EP2292751A1 (de) * | 2009-08-20 | 2011-03-09 | Roche Diagnostics GmbH | Stabilisierung von Enzymen mit stabilen Coenzymen |
| US8787944B2 (en) | 2011-08-18 | 2014-07-22 | Rivada Research, Llc | Method and system for providing enhanced location based information for wireless handsets |
| EP2636750A1 (en) | 2012-03-06 | 2013-09-11 | Roche Diagniostics GmbH | Compatible solute ectoine as well as derivatives thereof for enzyme stabilization |
| CN104704367A (zh) * | 2012-08-09 | 2015-06-10 | 基础服务农业研究院 | 膜组件和包含这种膜组件的侧流免疫测定装置 |
| US8921061B2 (en) | 2012-11-02 | 2014-12-30 | Roche Diagnostics Operations, Inc. | Reagent materials and associated test elements |
| EP2770064A1 (de) * | 2013-02-22 | 2014-08-27 | F. Hoffmann-La Roche AG | Hocheffiziente Herstellung von Blutglucose-Teststreifen |
| KR101847758B1 (ko) | 2014-01-24 | 2018-04-10 | 에프. 호프만-라 로슈 아게 | 유니- 및 노-코드 테스트 스트라이프 제조 방법 |
| PL3523639T3 (pl) | 2016-10-05 | 2025-03-17 | F. Hoffmann-La Roche Ag | Odczynniki wykrywające i układy elektrod do elementów diagnostycznych testów wieloanalitowych oraz sposoby ich zastosowania |
| EP3339431A1 (en) * | 2016-12-22 | 2018-06-27 | Roche Diabetes Care GmbH | Glucose dehydrogenase variants with improved properties |
| US12215359B2 (en) | 2019-05-01 | 2025-02-04 | Codexis, Inc. | Engineered glucose dehydrogenases and methods for the reductive amination of ketone and amine compounds |
| WO2020242967A1 (en) * | 2019-05-28 | 2020-12-03 | W. L. Gore & Associates, Inc. | Stabilized medical device and method for making it |
| US11918355B2 (en) * | 2019-08-30 | 2024-03-05 | Abbott Diabetes Care Inc. | Analyte sensors and sensing methods for the detection of alcohol |
Family Cites Families (21)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| DE2061984C3 (de) | 1970-12-16 | 1974-04-11 | Boehringer Mannheim Gmbh, 6800 Mannheim | Reagens zur Bestimmung der Lactat-Dehydrogenase im Farbtest |
| US5032506A (en) | 1986-12-16 | 1991-07-16 | Enzymatics, Inc. | Color control system |
| US5609718A (en) | 1995-09-29 | 1997-03-11 | Micron Technology, Inc. | Method and apparatus for measuring a change in the thickness of polishing pads used in chemical-mechanical planarization of semiconductor wafers |
| 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 |
| US6710770B2 (en) * | 2000-02-11 | 2004-03-23 | Canesta, Inc. | Quasi-three-dimensional method and apparatus to detect and localize interaction of user-object and virtual transfer device |
| WO2001094370A1 (en) | 2000-06-07 | 2001-12-13 | Wako Pure Chemical Industries, Ltd. | Coenzyme derivatives and enzymes appropriate therefor |
| BR0309947B1 (pt) | 2002-05-16 | 2013-11-26 | Processo e dispositivo para produção de camadas de polímero sobre um suporte transparente, sua utilização e processo para produção de um sensor | |
| MXPA06001719A (es) | 2003-08-11 | 2006-05-19 | Codexis Inc | Polipeptidos de glucosa deshidrogenasa mejorados, y polinucleotidos relacionados. |
| DE102006035020B4 (de) * | 2005-07-28 | 2018-08-23 | Roche Diabetes Care Gmbh | Stabilisierung von NAD/NADH |
| US7553615B2 (en) | 2005-07-28 | 2009-06-30 | Roche Diagnostics Operations, Inc. | Compounds, methods, complexes, apparatuses and uses relating to stabile forms of NAD/NADH |
| DE102005035461A1 (de) * | 2005-07-28 | 2007-02-15 | Roche Diagnostics Gmbh | Stabile NAD/NADH-Derivate |
| US20070196899A1 (en) | 2005-11-29 | 2007-08-23 | Sony Corporation | Mutant protein having diaphorase activity |
| GB0625671D0 (en) | 2006-12-21 | 2007-01-31 | Oxford Biosensors Ltd | Protein formulation |
| EP1964927A1 (de) * | 2007-02-27 | 2008-09-03 | F. Hoffmann-La Roche AG | Chinone als Mediatoren für photometrische Teste |
| EP2093284A1 (de) * | 2008-02-19 | 2009-08-26 | F.Hoffmann-La Roche Ag | Stabilisierung von Dehydrogenasen mit stabilen Coenzymen |
| EP2287605A1 (de) * | 2009-08-20 | 2011-02-23 | Roche Diagnostics GmbH | Vereinfachte Magazinierung integrierter Systeme |
| EP2292751A1 (de) * | 2009-08-20 | 2011-03-09 | Roche Diagnostics GmbH | Stabilisierung von Enzymen mit stabilen Coenzymen |
| EP2333544A1 (de) * | 2009-12-11 | 2011-06-15 | F. Hoffmann-La Roche AG | Sterilisierbare Chemie für Testelemente |
| WO2011073258A1 (de) * | 2009-12-16 | 2011-06-23 | F. Hoffmann-La Roche Ag | Detektion der zersetzung von enzymen in einem testelement durch kontrollierte freisetzung von geschütztem analyt |
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| CN102471767B (zh) | 2018-02-16 |
| CN102471767A (zh) | 2012-05-23 |
| CA2770249C (en) | 2015-04-28 |
| KR20120064076A (ko) | 2012-06-18 |
| US20170073661A1 (en) | 2017-03-16 |
| US20120276565A1 (en) | 2012-11-01 |
| JP2013502212A (ja) | 2013-01-24 |
| EP2292751A1 (de) | 2011-03-09 |
| WO2011020856A1 (de) | 2011-02-24 |
| KR20150070443A (ko) | 2015-06-24 |
| EP2467478A1 (de) | 2012-06-27 |
| MX2012001946A (es) | 2012-04-02 |
| KR101554457B1 (ko) | 2015-09-30 |
| CA2770249A1 (en) | 2011-02-24 |
| EP2467478B1 (de) | 2015-09-16 |
| US9540702B2 (en) | 2017-01-10 |
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