IE81141B1 - Procaryotic carbonyl hydrolases - Google Patents
Procaryotic carbonyl hydrolasesInfo
- Publication number
- IE81141B1 IE81141B1 IE156784A IE156784A IE81141B1 IE 81141 B1 IE81141 B1 IE 81141B1 IE 156784 A IE156784 A IE 156784A IE 156784 A IE156784 A IE 156784A IE 81141 B1 IE81141 B1 IE 81141B1
- Authority
- IE
- Ireland
- Prior art keywords
- enzyme
- subtilisin
- dna
- mutant
- mutation
- Prior art date
Links
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Classifications
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- C—CHEMISTRY; METALLURGY
- C11—ANIMAL OR VEGETABLE OILS, FATS, FATTY SUBSTANCES OR WAXES; FATTY ACIDS THEREFROM; DETERGENTS; CANDLES
- C11D—DETERGENT COMPOSITIONS; USE OF SINGLE SUBSTANCES AS DETERGENTS; SOAP OR SOAP-MAKING; RESIN SOAPS; RECOVERY OF GLYCEROL
- C11D3/00—Other compounding ingredients of detergent compositions covered in group C11D1/00
- C11D3/16—Organic compounds
- C11D3/38—Products with no well-defined composition, e.g. natural products
- C11D3/386—Preparations containing enzymes, e.g. protease or amylase
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- 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
- C12N1/00—Microorganisms, e.g. protozoa; Compositions thereof; Processes of propagating, maintaining or preserving microorganisms or compositions thereof; Processes of preparing or isolating a composition containing a microorganism; Culture media therefor
- C12N1/20—Bacteria; Culture media therefor
- C12N1/205—Bacterial isolates
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- 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
- C12N15/00—Mutation or genetic engineering; DNA or RNA concerning genetic engineering, vectors, e.g. plasmids, or their isolation, preparation or purification; Use of hosts therefor
- C12N15/09—Recombinant DNA-technology
- C12N15/10—Processes for the isolation, preparation or purification of DNA or RNA
- C12N15/102—Mutagenizing nucleic acids
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- 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
- C12N15/00—Mutation or genetic engineering; DNA or RNA concerning genetic engineering, vectors, e.g. plasmids, or their isolation, preparation or purification; Use of hosts therefor
- C12N15/09—Recombinant DNA-technology
- C12N15/63—Introduction of foreign genetic material using vectors; Vectors; Use of hosts therefor; Regulation of expression
- C12N15/74—Vectors or expression systems specially adapted for prokaryotic hosts other than E. coli, e.g. Lactobacillus, Micromonospora
- C12N15/75—Vectors or expression systems specially adapted for prokaryotic hosts other than E. coli, e.g. Lactobacillus, Micromonospora for Bacillus
-
- 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
- C12N9/14—Hydrolases (3)
- C12N9/48—Hydrolases (3) acting on peptide bonds (3.4)
- C12N9/50—Proteinases, e.g. Endopeptidases (3.4.21-3.4.25)
- C12N9/52—Proteinases, e.g. Endopeptidases (3.4.21-3.4.25) derived from bacteria or Archaea
- C12N9/54—Proteinases, e.g. Endopeptidases (3.4.21-3.4.25) derived from bacteria or Archaea bacteria being Bacillus
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12R—INDEXING SCHEME ASSOCIATED WITH SUBCLASSES C12C - C12Q, RELATING TO MICROORGANISMS
- C12R2001/00—Microorganisms ; Processes using microorganisms
- C12R2001/01—Bacteria or Actinomycetales ; using bacteria or Actinomycetales
- C12R2001/07—Bacillus
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- Chemical Kinetics & Catalysis (AREA)
- Crystallography & Structural Chemistry (AREA)
- Oil, Petroleum & Natural Gas (AREA)
- Tropical Medicine & Parasitology (AREA)
- Virology (AREA)
- Micro-Organisms Or Cultivation Processes Thereof (AREA)
- Enzymes And Modification Thereof (AREA)
- Detergent Compositions (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
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Applications Claiming Priority (6)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| US50741983A | 1983-06-24 | 1983-06-24 | |
| US61461684A | 1984-05-29 | 1984-05-29 | |
| US61461584A | 1984-05-29 | 1984-05-29 | |
| US61461784A | 1984-05-29 | 1984-05-29 | |
| US61449184A | 1984-05-29 | 1984-05-29 | |
| US06/614,612 US4760025A (en) | 1984-05-29 | 1984-05-29 | Modified enzymes and methods for making same |
Publications (2)
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|---|---|
| IE841567L IE841567L (en) | 1984-12-24 |
| IE81141B1 true IE81141B1 (en) | 2000-04-05 |
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| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| IE156784A IE81141B1 (en) | 1983-06-24 | 1984-06-21 | Procaryotic carbonyl hydrolases |
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| Publication number | Priority date | Publication date | Assignee | Title |
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| IE81141B1 (en) | 1983-06-24 | 2000-04-05 | Genencor Int | Procaryotic carbonyl hydrolases |
| CA1311429C (en) * | 1983-07-06 | 1992-12-15 | Vasantha Nagarajan | Vector for polypeptides in bacilli |
| JPH0659224B2 (ja) * | 1983-09-12 | 1994-08-10 | 工業技術院長 | Ｄνａ塩基配列及びそのｄνａ塩基配列を含む組換え体プラスミドの創製法 |
| EP0462632A1 (en) * | 1983-10-28 | 1991-12-27 | Genetics Institute, Inc. | Method for producing a desired human protein by recombinant DNA techniques |
| EP0162067B1 (en) * | 1983-10-28 | 1992-07-15 | Genetics Institute, Inc. | Production of factor viii and related products |
| EP0149241B1 (en) * | 1983-12-28 | 1991-03-27 | Agency Of Industrial Science And Technology | Dna base sequence containing regions involved in the production and secretion of a protein, recombinant dna including the whole or a part of the dna base sequence, and method of producing proteins by use of the recombinant dna |
| US5185258A (en) * | 1984-05-29 | 1993-02-09 | Genencor International, Inc. | Subtilisin mutants |
| US5411873A (en) * | 1984-05-29 | 1995-05-02 | Genencor, Inc. | Process for producing heterologous polypeptides |
| US5972682A (en) * | 1984-05-29 | 1999-10-26 | Genencor International, Inc. | Enzymatically active modified subtilisins |
| US4801537A (en) * | 1984-06-08 | 1989-01-31 | Genex Corporation | Vector for expression of polypeptides in bacilli |
| US5840522A (en) * | 1984-09-20 | 1998-11-24 | Chiron Corporation | Recombinant lectins |
| US4828994A (en) * | 1984-09-21 | 1989-05-09 | Genex Corporation | Bacillus strains with reduced extracellular protease levels |
| CA1340265C (en) * | 1985-01-18 | 1998-12-15 | Kirston E. Koths | Oxidation resistant muteins |
| US4752585A (en) * | 1985-12-17 | 1988-06-21 | Cetus Corporation | Oxidation-resistant muteins |
| US6084073A (en) * | 1985-03-25 | 2000-07-04 | Chiron Corporation | Recombinant ricin toxin |
| EP0316018A3 (en) * | 1985-03-29 | 1989-07-26 | Cetus Oncology Corporation | Modification of dna sequences |
| DE3685769T2 (de) * | 1985-04-15 | 1993-01-21 | Procter & Gamble | Fluessige reinigungsmittel mit einer oberflaechenaktiven verbindung, einem proteolytischen enzym und borsaeure. |
| EP0199404B1 (en) * | 1985-04-15 | 1992-06-24 | The Procter & Gamble Company | Liquid detergents containing anionic surfactant, builder and proteolytic enzyme |
| IT1186750B (it) * | 1985-07-10 | 1987-12-16 | Eniricerche Spa | Vettore di clonaggio,molecole di dna ricombinante,ceppi di bacillus subtilis trasformati con dette molecole e metodi per l'espressione di geni eterologhi e produzione e secrezione di proteine codificate da detti geni |
| DE3527913A1 (de) * | 1985-08-03 | 1987-02-12 | Henkel Kgaa | Alkalische protease, verfahren zur herstellung von hybridvektoren und genetisch transformierte mikroorganismen |
| EP0254735B2 (en) * | 1986-01-15 | 1998-06-17 | Amgen Inc. | METHOD FOR PRODUCTION OF THERMALLY STABLE AND pH STABLE SUBTILISIN ANALOGS |
| US4908773A (en) * | 1987-04-06 | 1990-03-13 | Genex Corporation | Computer designed stabilized proteins and method for producing same |
| US5013657A (en) * | 1988-04-12 | 1991-05-07 | Bryan Philip N | Subtilisin mutations |
| SG30639G (en) * | 1986-04-30 | 1995-09-01 | Genencor Int | Non-human carbonyl hydrolase mutants DNA sequences and vectors encoding same and hosts transformed with said vectors |
| DE3781017T2 (de) * | 1986-05-06 | 1993-03-18 | Univ Leland Stanford Junior | Cytotoxische zusammensetzung aus "killer"-zellen. |
| US5364554A (en) * | 1986-06-09 | 1994-11-15 | The Clorox Company | Proteolytic perhydrolysis system and method of use for bleaching |
| EP0260350B1 (en) * | 1986-09-05 | 1992-02-12 | Cetus Oncology Corporation | Oxidation-resistant interferon-beta muteins and their production; formulations containing such muteins |
| NZ221627A (en) * | 1986-09-09 | 1993-04-28 | Genencor Inc | Preparation of enzymes, modifications, catalytic triads to alter ratios or transesterification/hydrolysis ratios |
| PT86864B (pt) * | 1987-02-27 | 1992-05-29 | Gist Brocades Nv | Processo para clonagem molecular e expressao de genes que codificam para enzimas proteoliticas |
| EP0896062A3 (en) * | 1987-02-27 | 1999-04-07 | Genencor International, Inc. | Transformation of alkalophilic bacillus strains |
| RU2091487C1 (ru) * | 1987-02-27 | 1997-09-27 | Гист-Брокейдс Н.В. | Способ получения штамма bacillus, содержащего две копии последовательности днк, кодирующей фермент с гидролазной активностью |
| EP0285123A3 (en) * | 1987-04-03 | 1989-02-01 | Stabra AG | A method for complete mutagenesis of nucleic acids |
| US4853871A (en) * | 1987-04-06 | 1989-08-01 | Genex Corporation | Computer-based method for designing stablized proteins |
| ATE184316T1 (de) * | 1987-04-06 | 1999-09-15 | Novo Nordisk As | Regelung von elektrostatischen interaktionen an metallionen-bindungsstellen zur stabilisierung von proteinen |
| US4914031A (en) * | 1987-04-10 | 1990-04-03 | Amgen, Inc. | Subtilisin analogs |
| IT1228925B (it) * | 1987-08-07 | 1991-07-10 | Eniricerche Spa | Procedimento per la preparazione dell'ormone della crescita umano |
| US5041378A (en) * | 1987-08-11 | 1991-08-20 | Cetus Corporation | Procaryotic xylose isomerase muteins |
| US4939666A (en) * | 1987-09-02 | 1990-07-03 | Genex Corporation | Incremental macromolecule construction methods |
| US4966846A (en) * | 1987-10-01 | 1990-10-30 | W. R. Grace & Co.-Conn. | Molecular cloning and expression of a vibrio proteolyticus neutral protease gene |
| DK571587D0 (da) * | 1987-11-02 | 1987-11-02 | Novo Industri As | Enzymatisk detergentsammensaetning |
| GB8727772D0 (en) * | 1987-11-27 | 1987-12-31 | Celltech Ltd | Host cells |
| US4865983A (en) * | 1987-12-04 | 1989-09-12 | W. R. Grace & Co.-Conn. | Cleaning compositions containing protease produced by vibrio and method of use |
| EP0319759B1 (en) * | 1987-12-11 | 1993-01-07 | Abbott Laboratories | Method for mutagenesis by oligonucleotide-directed repair of a strand break |
| DK6488D0 (da) * | 1988-01-07 | 1988-01-07 | Novo Industri As | Enzymer |
| US5324653A (en) * | 1988-02-11 | 1994-06-28 | Gist-Brocades N.V. | Recombinant genetic means for the production of serine protease muteins |
| US6287841B1 (en) | 1988-02-11 | 2001-09-11 | Genencor International, Inc. | High alkaline serine protease |
| CN1056187C (zh) | 1988-02-11 | 2000-09-06 | 金克克国际有限公司 | 新的蛋白水解酶及其在洗涤剂中的应用 |
| US5246849A (en) * | 1988-04-12 | 1993-09-21 | Enzon, Inc. | Thermally stable serine proteases |
| US5118623A (en) * | 1988-05-27 | 1992-06-02 | Solvay Enzymes, Inc. | Bleach stable enzymes |
| CA1333777C (en) * | 1988-07-01 | 1995-01-03 | Randy M. Berka | Aspartic proteinase deficient filamentous fungi |
| HU200796B (en) * | 1988-07-14 | 1990-08-28 | Richter Gedeon Vegyeszet | Process for producing expression vectors ensuring insertion of nucleotide sequences into e. coli chromosome |
| US5665587A (en) * | 1989-06-26 | 1997-09-09 | Novo Nordisk A/S | Modified subtilisins and detergent compositions containing same |
| GB8915658D0 (en) * | 1989-07-07 | 1989-08-23 | Unilever Plc | Enzymes,their production and use |
| US5658871A (en) * | 1989-07-07 | 1997-08-19 | Lever Brothers Company, Division Of Conopco, Inc. | Microbial lipase muteins and detergent compositions comprising same |
| NL8902010A (nl) * | 1989-08-04 | 1991-03-01 | Nl Zuivelonderzoek Inst | Dna-fragment met ten minste een protease-gen, een dergelijk dna-fragment bevattende cloneringsvektor, een gastheercel getransformeerd met een dusdanig opgebouwde cloneringsvektor, alsmede de met dergelijke gastheercellen geproduceerde proteasen resp. bereide produkten zoals voedingsmiddelen. |
| ES2095233T3 (es) * | 1989-08-11 | 1997-02-16 | Gist Brocades Nv | Produccion eficaz de proteasa mutante. |
| US5352603A (en) * | 1989-08-31 | 1994-10-04 | Kali-Chemie Ag | Highly alkaline proteases |
| DE4023458A1 (de) * | 1989-08-31 | 1991-03-07 | Kali Chemie Ag | Neue hochalkalische proteasen |
| US6271012B1 (en) * | 1989-10-11 | 2001-08-07 | Genencor International, Inc. | Protease muteins and their use in detergents |
| JPH0813271B2 (ja) * | 1989-11-27 | 1996-02-14 | 日本ケミカルリサーチ株式会社 | 線溶活性蛋白質およびその製造法 |
| US5030378A (en) * | 1990-01-02 | 1991-07-09 | The Procter & Gamble Company | Liquid detergents containing anionic surfactant, builder and proteolytic enzyme |
| FI102542B (fi) * | 1990-01-04 | 1998-12-31 | Plant Genetic Systems Nv | Muuttuneen pH-profiilin omaavat uudet glukoosi-isomeraasit |
| IT1239733B (it) * | 1990-02-23 | 1993-11-15 | Eniricerche Spa | Mutanti della proteasi neutra termostabili e mezzi e metodi per la loro preparazione |
| DK271490D0 (da) * | 1990-11-14 | 1990-11-14 | Novo Nordisk As | Detergentkomposition |
| DE4037530A1 (de) * | 1990-11-26 | 1992-05-27 | Henkel Kgaa | Faellungsverfahren fuer exocellulaere proteine |
| US5482849A (en) * | 1990-12-21 | 1996-01-09 | Novo Nordisk A/S | Subtilisin mutants |
| US5340735A (en) * | 1991-05-29 | 1994-08-23 | Cognis, Inc. | Bacillus lentus alkaline protease variants with increased stability |
| US5702931A (en) * | 1991-07-01 | 1997-12-30 | Berlex Laboratories, Inc. | Mutagenesis methods and compositions |
| US5770410A (en) * | 1992-01-30 | 1998-06-23 | Genzyme Corporation | Chiral synthesis with modified enzymes |
| WO1993015208A1 (en) * | 1992-01-30 | 1993-08-05 | Genzyme Limited | Chiral synthesis with modified enzymes |
| US5316935A (en) * | 1992-04-06 | 1994-05-31 | California Institute Of Technology | Subtilisin variants suitable for hydrolysis and synthesis in organic media |
| US5869644A (en) * | 1992-04-15 | 1999-02-09 | The Johns Hopkins University | Synthesis of diverse and useful collections of oligonucleotidies |
| JPH0657299A (ja) * | 1992-05-13 | 1994-03-01 | Procter & Gamble Co:The | 陰イオン界面活性剤とカルボキシレートビルダーとタンパク分解酵素とアルカノールアミノとを含有する液体洗剤 |
| ES2334590T3 (es) * | 1992-07-23 | 2010-03-12 | Novozymes A/S | Alfa-amilasa mutante, detergente y agente de lavado de vajilla. |
| NZ262623A (en) * | 1993-02-11 | 1998-03-25 | Genencor Int | Alpha-amylase mutant, dna and vectors encoding such and detergent compositions thereof |
| DK39093D0 (da) * | 1993-04-01 | 1993-04-01 | Novo Nordisk As | Enzym |
| US6436690B1 (en) * | 1993-09-15 | 2002-08-20 | The Procter & Gamble Company | BPN′ variants having decreased adsorption and increased hydrolysis wherein one or more loop regions are substituted |
| US6440717B1 (en) * | 1993-09-15 | 2002-08-27 | The Procter & Gamble Company | BPN′ variants having decreased adsorption and increased hydrolysis |
| ES2364776T3 (es) | 1994-02-24 | 2011-09-14 | HENKEL AG & CO. KGAA | Enzimas mejoradas y detergentes que las contienen. |
| EP0701605B2 (en) | 1994-02-24 | 2017-02-22 | Basf Se | Improved enzymes and detergents containing them |
| USH1468H (en) | 1994-04-28 | 1995-08-01 | Costa Jill B | Detergent compositions containing cellulase enzyme and selected perfumes for improved odor and stability |
| US6599730B1 (en) * | 1994-05-02 | 2003-07-29 | Procter & Gamble Company | Subtilisin 309 variants having decreased adsorption and increased hydrolysis |
| EP0693549A1 (en) | 1994-07-19 | 1996-01-24 | The Procter & Gamble Company | Solid bleach activator compositions |
| JPH10504197A (ja) * | 1994-08-11 | 1998-04-28 | ジェネンコア インターナショナル インコーポレーテッド | 改善洗浄用組成物 |
| GB9416841D0 (en) | 1994-08-19 | 1994-10-12 | Finnfeeds Int Ltd | An enzyme feed additive and animal feed including it |
| US5780285A (en) * | 1995-03-03 | 1998-07-14 | Genentech, Inc. | Subtilisin variants capable of cleaving substrates containing dibasic residues |
| US5837516A (en) * | 1995-03-03 | 1998-11-17 | Genentech, Inc. | Subtilisin variants capable of cleaving substrates containing basic residues |
| US6455295B1 (en) * | 1995-03-08 | 2002-09-24 | The Procter & Gamble Company | Subtilisin Carlsberg variants having decreased adsorption and increased hydrolysis |
| US6475765B1 (en) * | 1995-03-09 | 2002-11-05 | Procter & Gamble Company | Subtilisin DY variants having decreased adsorption and increased hydrolysis |
| IL117350A0 (en) * | 1995-03-09 | 1996-07-23 | Procter & Gamble | Proteinase k variants having decreased adsorption and increased hydrolysis |
| US6682924B1 (en) * | 1995-05-05 | 2004-01-27 | Novozymes A/S | Protease variants and compositions |
| ES2115338T3 (es) | 1995-07-13 | 1998-06-16 | Procter & Gamble | Composicion de espumacion para envasado. |
| EP0753567A1 (en) | 1995-07-14 | 1997-01-15 | The Procter & Gamble Company | Softening through the wash compositions |
| DE19530816A1 (de) | 1995-08-23 | 1997-02-27 | Cognis Bio Umwelt | Verwendung von mutierter Subtilisin-Protease in kosmetischen Produkten |
| EP0778342A1 (en) | 1995-12-06 | 1997-06-11 | The Procter & Gamble Company | Detergent compositions |
| EP0927240A1 (en) | 1996-05-03 | 1999-07-07 | The Procter & Gamble Company | Detergent compositions comprising polyamine polymers with improved soil dispersancy |
| US5858948A (en) * | 1996-05-03 | 1999-01-12 | Procter & Gamble Company | Liquid laundry detergent compositions comprising cotton soil release polymers and protease enzymes |
| US5958739A (en) * | 1996-06-06 | 1999-09-28 | Genencor International Inc. | Mutant α-amylase |
| BR9712114A (pt) | 1996-09-24 | 1999-08-31 | Procter & Gamble | Composições detergente líquidas para lavanderia contendo enzima proteolítica e inibidores de protease. |
| EP0929640A1 (en) * | 1996-09-24 | 1999-07-21 | The Procter & Gamble Company | Liquid detergents containing proteolytic enzyme and protease inhibitors |
| US6165966A (en) * | 1996-09-24 | 2000-12-26 | The Procter & Gamble Company | Liquid detergents containing proteolytic enzyme and protease inhibitors |
| KR19990076798A (ko) * | 1996-10-29 | 1999-10-15 | 요트.게.아. 롤페즈 | 텔레비젼 수상기 |
| WO1998020116A1 (en) | 1996-11-04 | 1998-05-14 | Novo Nordisk A/S | Subtilase variants and compositions |
| WO1998020115A1 (en) | 1996-11-04 | 1998-05-14 | Novo Nordisk A/S | Subtilase variants and compositions |
| BR9714453A (pt) | 1996-12-31 | 2000-03-21 | Procter & Gamble | as,espessadas |
| CA2276578A1 (en) * | 1996-12-31 | 1998-07-09 | Sherri L. Randall | Laundry detergent compositions with polyamide-polyamines |
| BR9714454A (pt) * | 1996-12-31 | 2000-03-21 | Procter & Gamble | endo fixadores de corante |
| BR9714455A (pt) | 1996-12-31 | 2000-03-21 | Procter & Gamble | e aquosas, de baixo custo com tensoativos aromáticos. |
| DE19717346C2 (de) * | 1997-04-24 | 1999-05-20 | Max Planck Gesellschaft | DNA-Sonden, Verfahren und Kit zur Identifizierung Antibiotika-resistenter Bakterienstämme |
| US6080568A (en) * | 1997-08-19 | 2000-06-27 | Genencor International, Inc. | Mutant α-amylase comprising modification at residues corresponding to A210, H405 and/or T412 in Bacillus licheniformis |
| CN100593036C (zh) | 1997-08-29 | 2010-03-03 | 诺沃奇梅兹有限公司 | 蛋白酶变体及组合物 |
| EP1012251A1 (en) | 1997-08-29 | 2000-06-28 | Novo Nordisk A/S | Protease variants and compositions |
| US6780629B2 (en) | 1997-11-21 | 2004-08-24 | Novozymes A/S | Subtilase enzymes |
| ATE298791T1 (de) | 1997-11-21 | 2005-07-15 | Novozymes As | Protease-varianten und zusammensetzungen |
| US6773907B2 (en) | 1997-11-21 | 2004-08-10 | Peter Kamp Hansen | Subtilase enzymes |
| EP1057015A1 (en) | 1997-12-20 | 2000-12-06 | Genencor International, Inc. | Accelerated stability test |
| BR9813766A (pt) | 1997-12-20 | 2000-10-24 | Genencor Int | Grânulo, e, processo para preparação de um grânulo. |
| AU745104B2 (en) | 1997-12-20 | 2002-03-14 | Genencor International, Inc. | Granule with hydrated barrier material |
| EP1021525A1 (en) | 1997-12-20 | 2000-07-26 | Genencor International, Inc. | Fluidized bed matrix granule |
| US6908757B1 (en) | 1998-03-26 | 2005-06-21 | The Procter & Gamble Company | Serine protease variants having amino acid deletions and substitutions |
| HK1041024A1 (zh) | 1998-10-27 | 2002-06-28 | 金克克国际有限公司 | 基质颗粒 |
| US6310027B1 (en) | 1998-11-13 | 2001-10-30 | Genencor International, Inc. | Fluidized bed low density granule |
| EP1803817B1 (en) | 1998-12-18 | 2011-04-06 | Novozymes A/S | Subtilase enzymes of the I-S1 and I-S2 sub-groups having an additional amino acid residue in an active site loop region |
| MXPA01006944A (es) | 1999-01-08 | 2003-09-10 | Genencor Int | Composiciones de baja densidad y materiales particulados que incluyen las mismas. |
| WO2000071685A1 (en) | 1999-05-20 | 2000-11-30 | Novozymes A/S | Subtilase enzymes of the i-s1 and i-s2 sub-groups having at least one additional amino acid residue between positions 132 and 133 |
| AU4392900A (en) | 1999-05-20 | 2000-12-12 | Novozymes A/S | Subtilase enzymes of the i-s1 and i-s2 sub-groups having at least one additionalamino acid residue between positions 127 and 128 |
| EP1183339B2 (en) | 1999-05-20 | 2013-03-13 | Novozymes A/S | Subtilase enzymes of the i-s1 and i-s2 sub-groups having at least one additional amino acid residue between positions 129 and 130 |
| WO2000071690A1 (en) | 1999-05-20 | 2000-11-30 | Novozymes A/S | Subtilase enzymes of the i-s1 and i-s2 sub-groups having at least one additional amino acid residue between positions 128 and 129 |
| ATE402996T1 (de) | 1999-05-20 | 2008-08-15 | Novozymes As | Subtilase-enzyme der i-s1 und i-s2 untergruppen mit wenigstens einem zusätzlichen aminosäurerest zwischen positionen 125 und 126 |
| EP1183340B1 (en) | 1999-05-20 | 2008-09-03 | Novozymes A/S | Subtilase enzymes of the i-s1 and i-s2 sub-groups having at least one additional amino acid residue between positions 126 and 127 |
| KR20020021397A (ko) | 1999-07-22 | 2002-03-20 | 데이비드 엠 모이어 | 규정된 에피토프 영역에 아미노산 결실 및 치환을 갖는서브틸리신 프로테아제 변이체 |
| KR20020021398A (ko) | 1999-07-22 | 2002-03-20 | 데이비드 엠 모이어 | 정의된 에피토프 구역에 아미노산 치환을 가진 서브틸리신프로테아제 변이체 |
| US6946128B1 (en) | 1999-07-22 | 2005-09-20 | The Procter & Gamble Company | Protease conjugates having sterically protected epitope regions |
| AU5928400A (en) | 1999-07-22 | 2001-02-13 | Procter & Gamble Company, The | Protease conjugates having sterically protected clip sites |
| US6558939B1 (en) | 1999-08-31 | 2003-05-06 | Novozymes, A/S | Proteases and variants thereof |
| US7217554B2 (en) | 1999-08-31 | 2007-05-15 | Novozymes A/S | Proteases and variants thereof |
| EP2336331A1 (en) | 1999-08-31 | 2011-06-22 | Novozymes A/S | Novel proteases and variants thereof |
| CN1375000A (zh) * | 1999-09-09 | 2002-10-16 | 宝洁公司 | 含有蛋白酶的洗涤剂组合物 |
| CN1398235A (zh) | 1999-09-22 | 2003-02-19 | 宝洁公司 | 手持液体容器 |
| DK1220887T3 (da) | 1999-10-15 | 2006-04-10 | Genencor Int | Proteinholdige granuler og granuleformuleringer |
| US6727085B2 (en) * | 1999-12-15 | 2004-04-27 | Fanoe Tina Sejersgaard | Subtilase variants having an improved wash performance on egg stains |
| US6855548B2 (en) | 2000-02-08 | 2005-02-15 | F. Hoffman-La Roche Ag | Use of acid-stable proteases in animal feed |
| US6960462B2 (en) | 2000-02-08 | 2005-11-01 | Dsm Ip Assets B.V | Use of acid-stable subtilisin proteases in animal feed |
| US6777218B1 (en) | 2000-03-14 | 2004-08-17 | Novozymes A/S | Subtilase enzymes having an improved wash performance on egg stains |
| US6872696B2 (en) | 2000-10-27 | 2005-03-29 | Genencor International, Inc. | Particle with substituted polyvinyl alcohol coating |
| US6803222B2 (en) * | 2000-11-22 | 2004-10-12 | Kao Corporation | Alkaline proteases |
| AU2002254374A1 (en) | 2001-03-23 | 2002-10-08 | Genencor International, Inc. | Proteins producing an altered immunogenic response and methods of making and using the same |
| US8076113B2 (en) * | 2001-04-02 | 2011-12-13 | Danisco Us Inc. | Method for producing granules with reduced dust potential comprising an antifoam agent |
| US7157416B2 (en) | 2001-07-20 | 2007-01-02 | Genencor International, Inc. | Stabilization of enzymes |
| US7153820B2 (en) | 2001-08-13 | 2006-12-26 | Ecolab Inc. | Solid detergent composition and method for solidifying a detergent composition |
| DE10153792A1 (de) | 2001-10-31 | 2003-05-22 | Henkel Kgaa | Neue Alkalische Protease-Varianten und Wasch- und Reinigungsmittel enthaltend diese neuen Alkalischen Protease-Varianten |
| DE10162727A1 (de) | 2001-12-20 | 2003-07-10 | Henkel Kgaa | Neue Alkalische Protease aus Bacillus gibsonii (DSM 14391) und Wasch-und Reinigungsmittel enthaltend diese neue Alkalische Protease |
| DE10162728A1 (de) | 2001-12-20 | 2003-07-10 | Henkel Kgaa | Neue Alkalische Protease aus Bacillus gibsonii (DSM 14393) und Wasch-und Reinigungsmittel enthaltend diese neue Alkalische Protease |
| DE10163884A1 (de) | 2001-12-22 | 2003-07-10 | Henkel Kgaa | Neue Alkalische Protease aus Bacillus sp. (DSM 14392) und Wasch- und Reinigungsmittel enthaltend diese neue Alkalische Protease |
| BR0215383A (pt) * | 2001-12-31 | 2006-11-28 | Genencor Int | proteases que produzem resposta imunogênica alterada e métodos de fabricação e uso das mesmas |
| AU2002353178C1 (en) * | 2001-12-31 | 2011-02-03 | Genencor International, Inc. | Proteases producing an altered immunological response and methods of making and using the same |
| CA2915148C (en) | 2002-03-29 | 2018-03-13 | Eugenio Ferrari | Enhanced protein expression in bacillus |
| CA2502304C (en) | 2002-10-08 | 2013-10-01 | Genencor International, Inc. | Phenolic binding peptides |
| US7888093B2 (en) * | 2002-11-06 | 2011-02-15 | Novozymes A/S | Subtilase variants |
| EP1594963B1 (en) | 2003-02-07 | 2007-07-25 | Novozymes A/S | Proteases |
| DE602004016314D1 (de) | 2003-05-07 | 2008-10-16 | Maxygen Inc | Enzymvarianten von subtilisin (subtilasen) |
| US7892808B2 (en) | 2003-10-10 | 2011-02-22 | Norozymes A/S | Protease variants |
| EP1678296B1 (en) | 2003-10-23 | 2011-07-13 | Novozymes A/S | Protease with improved stability in detergents |
| BRPI0511171A (pt) | 2004-05-17 | 2007-12-04 | Procter & Gamble | composição de alvejamento compreendendo um carboidrato oxidase |
| EP2258838A1 (en) | 2004-06-21 | 2010-12-08 | Novozymes A/S | Nocardiopsis proteases |
| JP4681283B2 (ja) | 2004-11-18 | 2011-05-11 | 独立行政法人海洋研究開発機構 | 新規な高アルカリプロテアーゼ及びその利用 |
| JP4485341B2 (ja) | 2004-12-20 | 2010-06-23 | 花王株式会社 | 組換え微生物 |
| EP1700904A1 (en) | 2005-03-11 | 2006-09-13 | Unilever N.V. | Liquid detergent composition |
| EP1700907A1 (en) | 2005-03-11 | 2006-09-13 | Unilever N.V. | Liquid bleaching composition |
| US7666963B2 (en) | 2005-07-21 | 2010-02-23 | Akzo Nobel N.V. | Hybrid copolymers |
| WO2007136469A2 (en) | 2006-04-14 | 2007-11-29 | Genencor International, Inc. | One-step treatment of textiles |
| US20090215663A1 (en) | 2006-04-20 | 2009-08-27 | Novozymes A/S | Savinase variants having an improved wash performance on egg stains |
| NO20073834L (no) | 2006-07-21 | 2008-01-22 | Akzo Nobel Chemicals Int Bv | Sulfonerte podede kopolymerer |
| NO20073821L (no) | 2006-07-21 | 2008-01-22 | Akzo Nobel Chemicals Int Bv | Podede kopolymerer med lav molekylvekt |
| US8093200B2 (en) | 2007-02-15 | 2012-01-10 | Ecolab Usa Inc. | Fast dissolving solid detergent |
| EP2147098B1 (en) | 2007-04-30 | 2013-07-17 | Danisco US Inc. | Use of protein hydrolysates to stabilize metalloprotease detergent formulations |
| SG148934A1 (en) | 2007-06-11 | 2009-01-29 | Novozymes As | A process for combined biopolishing and bleach clean-up |
| US8383589B2 (en) | 2007-07-09 | 2013-02-26 | The United States Of America, As Represented By The Secretary, Department Of Health And Human Services | Aegyptin and uses thereof |
| EP3438235A1 (en) | 2007-10-18 | 2019-02-06 | Ecolab USA Inc. | Pressed, waxy, solid cleaning compositions and methods of making them |
| CA2703975C (en) * | 2007-10-31 | 2018-01-09 | Danisco Us Inc. | Use and production of citrate-stable neutral metalloproteases |
| BRPI0908237A2 (pt) | 2008-02-14 | 2015-07-21 | Danisco Us Inc | Pequenos grânulos contendo enzima |
| US8153574B2 (en) | 2009-03-18 | 2012-04-10 | The Procter & Gamble Company | Structured fluid detergent compositions comprising dibenzylidene polyol acetal derivatives and detersive enzymes |
| US8293697B2 (en) | 2009-03-18 | 2012-10-23 | The Procter & Gamble Company | Structured fluid detergent compositions comprising dibenzylidene sorbitol acetal derivatives |
| WO2010138347A1 (en) | 2009-05-26 | 2010-12-02 | The Procter & Gamble Company | Aqueous liquid composition for pre-treating soiled dishware |
| DE102009027045A1 (de) * | 2009-06-19 | 2010-12-30 | Henkel Ag & Co. Kgaa | Neue Proteasen und Mittel enthaltend diese Proteasen |
| WO2011005623A1 (en) | 2009-07-09 | 2011-01-13 | The Procter & Gamble Company | Laundry detergent composition comprising low level of bleach |
| US20110009307A1 (en) | 2009-07-09 | 2011-01-13 | Alan Thomas Brooker | Laundry Detergent Composition Comprising Low Level of Sulphate |
| EP2459607B1 (en) | 2009-07-31 | 2021-04-14 | Nouryon Chemicals International B.V. | Hybrid copolymer compositions for personal care applications |
| KR101802988B1 (ko) | 2010-05-14 | 2017-12-14 | 헨켈 아이피 앤드 홀딩 게엠베하 | 중합체 함유 세정 조성물, 이의 제조 방법 및 용도 |
| WO2012022777A1 (en) * | 2010-08-19 | 2012-02-23 | Novozymes A/S | Induced sporulation screening method |
| JP6023180B2 (ja) | 2011-05-20 | 2016-11-09 | エコラボ ユーエスエー インコーポレイティド | 物品洗浄のための、アルカリ／酸交替系における非ホスフェート洗剤及び非リン酸 |
| US8758520B2 (en) | 2011-05-20 | 2014-06-24 | Ecolab Usa Inc. | Acid formulations for use in a system for warewashing |
| US8841246B2 (en) | 2011-08-05 | 2014-09-23 | Ecolab Usa Inc. | Cleaning composition containing a polysaccharide hybrid polymer composition and methods of improving drainage |
| US8636918B2 (en) | 2011-08-05 | 2014-01-28 | Ecolab Usa Inc. | Cleaning composition containing a polysaccharide hybrid polymer composition and methods of controlling hard water scale |
| US8853144B2 (en) | 2011-08-05 | 2014-10-07 | Ecolab Usa Inc. | Cleaning composition containing a polysaccharide graft polymer composition and methods of improving drainage |
| US8679366B2 (en) | 2011-08-05 | 2014-03-25 | Ecolab Usa Inc. | Cleaning composition containing a polysaccharide graft polymer composition and methods of controlling hard water scale |
| SG11201401383WA (en) | 2011-11-04 | 2014-08-28 | Akzo Nobel Chemicals Int Bv | Graft dendrite copolymers, and methods for producing the same |
| EP2773320B1 (en) | 2011-11-04 | 2016-02-03 | Akzo Nobel Chemicals International B.V. | Hybrid dendrite copolymers, compositions thereof and methods for producing the same |
| US9139800B2 (en) | 2011-12-13 | 2015-09-22 | Ecolab Usa Inc. | Concentrated warewashing compositions and methods |
| WO2014007229A1 (ja) * | 2012-07-06 | 2014-01-09 | 東洋紡株式会社 | 改変型アルカリホスファターゼ |
| BR112015001137A2 (pt) | 2012-07-26 | 2017-06-27 | Procter & Gamble | composições de limpeza líquidas com enzimas e baixo ph |
| US8945314B2 (en) | 2012-07-30 | 2015-02-03 | Ecolab Usa Inc. | Biodegradable stability binding agent for a solid detergent |
| US9745543B2 (en) | 2012-09-10 | 2017-08-29 | Ecolab Usa Inc. | Stable liquid manual dishwashing compositions containing enzymes |
| EP2904085B1 (en) | 2012-10-04 | 2018-11-07 | Ecolab USA Inc. | Pre-soak technology for laundry and other hard surface cleaning |
| US9139458B2 (en) | 2013-03-15 | 2015-09-22 | Janet Angel | Compositions and methods of use |
| ES2905972T3 (es) | 2013-09-09 | 2022-04-12 | Ecolab Usa Inc | Eliminación sinérgica de manchas a través de una nueva combinación de quelantes |
| CN105518118B (zh) | 2013-09-09 | 2019-09-17 | 艺康美国股份有限公司 | 通过螯合剂组合来协同去污 |
| CA2928577C (en) | 2013-10-24 | 2018-11-27 | Tobias Neil FOSTER | Compositions and methods for removing soils from surfaces |
| US9365805B2 (en) | 2014-05-15 | 2016-06-14 | Ecolab Usa Inc. | Bio-based pot and pan pre-soak |
| EP3174446B1 (en) | 2014-08-01 | 2019-01-30 | Ecolab USA Inc. | A method of manual surface cleaning using cleaning textiles and of washing said cleaning textiles |
| US10577571B2 (en) | 2016-11-08 | 2020-03-03 | Ecolab Usa Inc. | Non-aqueous cleaner for vegetable oil soils |
| WO2020099491A1 (en) | 2018-11-14 | 2020-05-22 | Novozymes A/S | Oral care composition comprising a polypeptide having dnase activity |
| WO2021022045A1 (en) | 2019-07-31 | 2021-02-04 | Ecolab Usa Inc. | Personal protective equipment free delimer compositions |
| US11873465B2 (en) | 2019-08-14 | 2024-01-16 | Ecolab Usa Inc. | Methods of cleaning and soil release of highly oil absorbing substrates employing optimized extended chain nonionic surfactants |
| CN110760466B (zh) * | 2019-11-18 | 2021-04-20 | 山东隆科特酶制剂有限公司 | 一株产耐高温中性蛋白酶的枯草芽孢杆菌及其应用 |
| US12152220B2 (en) | 2020-07-06 | 2024-11-26 | Ecolab Usa Inc. | PEG-modified castor oil based compositions for microemulsifying and removing multiple oily soils |
| US20220000726A1 (en) | 2020-07-06 | 2022-01-06 | Ecolab Usa Inc. | Foaming mixed alcohol/water compositions comprising a structured alkoxylated siloxane |
| AU2021305611B2 (en) | 2020-07-06 | 2024-06-13 | Ecolab Usa Inc. | Foaming mixed alcohol/water compositions comprising a combination of alkyl siloxane and a hydrotrope/solubilizer |
| JP2023539234A (ja) | 2020-08-24 | 2023-09-13 | ノボザイムス アクティーゼルスカブ | フルクタナーゼを含む口腔ケア組成物 |
| US20240247209A1 (en) | 2021-05-18 | 2024-07-25 | Nouryon Chemicals International B.V. | Polyester polyquats in cleaning applications |
| EP4341317A1 (en) | 2021-05-20 | 2024-03-27 | Nouryon Chemicals International B.V. | Manufactured polymers having altered oligosaccharide or polysaccharide functionality or narrowed oligosaccharide distribution, processes for preparing them, compositions containing them, and methods of using them |
| US20240287409A1 (en) | 2021-06-30 | 2024-08-29 | Nouryon Chemicals International B.V. | Chelate-amphoteric surfactant liquid concentrates and use thereof in cleaning applications |
| WO2023057367A1 (en) | 2021-10-08 | 2023-04-13 | Unilever Ip Holdings B.V. | Laundry composition |
| WO2024020445A1 (en) | 2022-07-20 | 2024-01-25 | Ecolab Usa Inc. | Novel nonionic extended surfactants, compositions and methods of use thereof |
Family Cites Families (26)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US362957A (en) * | 1887-05-17 | haig-ht | ||
| US3557002A (en) | 1967-11-15 | 1971-01-19 | Procter & Gamble | Stabilized aqueous enzyme preparation |
| US3558498A (en) | 1967-11-29 | 1971-01-26 | Procter & Gamble | Granular detergent composition containing enzymes and environmental control components |
| GB1240058A (en) | 1968-04-12 | 1971-07-21 | Procter & Gamble | Enzyme-containing detergent compositions |
| US3623957A (en) | 1970-01-21 | 1971-11-30 | Baxter Laboratories Inc | Preparation of microbial alkaline protease by fermentation with bacillus subtilis, variety licheniformis |
| BE785666A (fr) | 1971-07-01 | 1973-01-02 | Procter & Gamble | Procede pour la production de compositions enzymatiques en granules |
| BE792982A (en) | 1971-12-20 | 1973-06-19 | Procter & Gamble Europ | Proteolytic enzymes detergent - contg cationic and anionic surfactants |
| US4011169A (en) | 1973-06-29 | 1977-03-08 | The Procter & Gamble Company | Stabilization and enhancement of enzymatic activity |
| DE2709476A1 (de) | 1976-03-08 | 1977-09-15 | Procter & Gamble Europ | Fluessiges, enzymhaltiges wasch- und reinigungsmittel |
| US4090973A (en) | 1976-06-24 | 1978-05-23 | The Procter & Gamble Company | Method for making stable detergent compositions |
| DE2633601A1 (de) | 1976-07-27 | 1978-02-02 | Henkel Kgaa | Fluessiges, als wasch- und reinigungsmittel verwendbares, enzymhaltiges konzentrat |
| GB1603640A (en) | 1977-07-20 | 1981-11-25 | Gist Brocades Nv | Enzyme particles |
| US4261868A (en) | 1979-08-08 | 1981-04-14 | Lever Brothers Company | Stabilized enzymatic liquid detergent composition containing a polyalkanolamine and a boron compound |
| US4302544A (en) * | 1979-10-15 | 1981-11-24 | University Of Rochester | Asporogenous mutant of B. subtilis for use as host component of HV1 system |
| US4318818A (en) | 1979-11-09 | 1982-03-09 | The Procter & Gamble Company | Stabilized aqueous enzyme composition |
| JPS5950280B2 (ja) | 1980-10-24 | 1984-12-07 | 花王株式会社 | 酵素入り漂白剤組成物 |
| JPS5786299A (en) * | 1980-11-19 | 1982-05-29 | Dai Ichi Seiyaku Co Ltd | Plasmid and its preparation |
| IE52434B1 (en) * | 1981-01-15 | 1987-10-28 | Cpc International Inc | A process for cloning the gene coding for a thermostable alpha-amylase into escherichia coli and bacillus subtilis |
| US4404128A (en) | 1981-05-29 | 1983-09-13 | The Procter & Gamble Company | Enzyme detergent composition |
| DE3122216A1 (de) * | 1981-06-04 | 1982-12-23 | Boehringer Mannheim Gmbh, 6800 Mannheim | Verfahren zur herstellung eines mikroorganismus, welcher (alpha)-galactosidase, aber keine invertase bildet, so erhaltener mikroorganismus und seine verwendung |
| DE3264685D1 (en) | 1981-11-13 | 1985-08-14 | Unilever Nv | Enzymatic liquid cleaning composition |
| JPS58162291A (ja) * | 1982-03-23 | 1983-09-26 | Res Dev Corp Of Japan | 耐熱性プロテア−ゼの製造法 |
| IL68366A (en) * | 1982-04-15 | 1990-08-31 | Genentech Inc | Process for expressing a gene encoding a protein comprising the enzymatic portion of human urokinase in a microorganism or cell culture |
| JPS5959190A (ja) * | 1982-09-29 | 1984-04-04 | Agency Of Ind Science & Technol | プロテア−ゼの製造法 |
| DK135983D0 (da) * | 1983-03-25 | 1983-03-25 | Novo Industri As | Maltogen amylaseenzymprodukt og fremgangsmade til dets fremstilling og anvendelse |
| IE81141B1 (en) | 1983-06-24 | 2000-04-05 | Genencor Int | Procaryotic carbonyl hydrolases |
-
1984
- 1984-06-21 IE IE156784A patent/IE81141B1/en unknown
- 1984-06-21 NZ NZ208612A patent/NZ208612A/en unknown
- 1984-06-22 AT AT87200689T patent/ATE60356T1/de not_active IP Right Cessation
- 1984-06-22 JP JP59129928A patent/JP2594533B2/ja not_active Expired - Lifetime
- 1984-06-22 EP EP84304252A patent/EP0130756B2/en not_active Expired - Lifetime
- 1984-06-22 EP EP87200690A patent/EP0246678B1/en not_active Expired - Lifetime
- 1984-06-22 DE DE87200690T patent/DE3486139T2/de not_active Expired - Fee Related
- 1984-06-22 DK DK198403059A patent/DK175278B1/da not_active IP Right Cessation
- 1984-06-22 DE DE8484304252T patent/DE3484079D1/de not_active Expired - Lifetime
- 1984-06-22 AT AT84304252T patent/ATE60797T1/de not_active IP Right Cessation
- 1984-06-22 DE DE8787200689T patent/DE3484019D1/de not_active Expired - Lifetime
- 1984-06-22 EP EP87200689A patent/EP0247647B1/en not_active Expired
- 1984-06-22 EP EP89202584A patent/EP0357157A3/en not_active Withdrawn
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1993
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- 1993-07-08 DK DK93823A patent/DK82393D0/da not_active Application Discontinuation
- 1993-07-29 HK HK754/93A patent/HK75493A/en not_active IP Right Cessation
- 1993-07-29 HK HK753/93A patent/HK75393A/en not_active IP Right Cessation
- 1993-09-23 HK HK992/93A patent/HK99293A/en not_active IP Right Cessation
- 1993-09-30 JP JP5244823A patent/JP2889095B2/ja not_active Expired - Lifetime
- 1993-09-30 JP JP5244837A patent/JPH06315378A/ja active Pending
Also Published As
| Publication number | Publication date |
|---|---|
| JP2889095B2 (ja) | 1999-05-10 |
| DE3484019D1 (de) | 1991-02-28 |
| HK75493A (en) | 1993-08-06 |
| DK305984D0 (da) | 1984-06-22 |
| DE3486139T2 (de) | 1993-11-11 |
| EP0247647A1 (en) | 1987-12-02 |
| NZ208612A (en) | 1991-09-25 |
| DK305984A (da) | 1985-02-18 |
| EP0130756A1 (en) | 1985-01-09 |
| DK82393A (da) | 1993-07-08 |
| EP0246678A1 (en) | 1987-11-25 |
| JPH06315378A (ja) | 1994-11-15 |
| DK175278B1 (da) | 2004-08-02 |
| ATE60356T1 (de) | 1991-02-15 |
| EP0247647B1 (en) | 1991-01-23 |
| DK175768B1 (da) | 2005-02-14 |
| EP0357157A3 (en) | 1990-03-28 |
| JPH06319534A (ja) | 1994-11-22 |
| HK75393A (en) | 1993-08-06 |
| DK82393D0 (da) | 1993-07-08 |
| DE3484079D1 (de) | 1991-03-14 |
| DE3486139D1 (GUID-C5D7CC26-194C-43D0-91A1-9AE8C70A9BFF.html) | 1993-06-03 |
| HK99293A (en) | 1993-09-30 |
| JPS6070075A (ja) | 1985-04-20 |
| IE841567L (en) | 1984-12-24 |
| DK82293D0 (da) | 1993-07-08 |
| EP0130756B2 (en) | 2000-06-28 |
| EP0130756B1 (en) | 1991-02-06 |
| EP0357157A2 (en) | 1990-03-07 |
| EP0246678B1 (en) | 1993-04-28 |
| JP2594533B2 (ja) | 1997-03-26 |
| DK82293A (da) | 1993-07-08 |
| ATE60797T1 (de) | 1991-02-15 |
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