AU2010340358B2 - Recombinant butyrylcholinesterases and truncates thereof - Google Patents
Recombinant butyrylcholinesterases and truncates thereof Download PDFInfo
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- AU2010340358B2 AU2010340358B2 AU2010340358A AU2010340358A AU2010340358B2 AU 2010340358 B2 AU2010340358 B2 AU 2010340358B2 AU 2010340358 A AU2010340358 A AU 2010340358A AU 2010340358 A AU2010340358 A AU 2010340358A AU 2010340358 B2 AU2010340358 B2 AU 2010340358B2
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Classifications
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- 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
- C12N15/11—DNA or RNA fragments; Modified forms thereof; Non-coding nucleic acids having a biological activity
- C12N15/52—Genes encoding for enzymes or proenzymes
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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
- C12N9/14—Hydrolases (3)
- C12N9/16—Hydrolases (3) acting on ester bonds (3.1)
- C12N9/18—Carboxylic ester hydrolases (3.1.1)
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- C07—ORGANIC CHEMISTRY
- C07H—SUGARS; DERIVATIVES THEREOF; NUCLEOSIDES; NUCLEOTIDES; NUCLEIC ACIDS
- C07H21/00—Compounds containing two or more mononucleotide units having separate phosphate or polyphosphate groups linked by saccharide radicals of nucleoside groups, e.g. nucleic acids
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- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07H—SUGARS; DERIVATIVES THEREOF; NUCLEOSIDES; NUCLEOTIDES; NUCLEIC ACIDS
- C07H21/00—Compounds containing two or more mononucleotide units having separate phosphate or polyphosphate groups linked by saccharide radicals of nucleoside groups, e.g. nucleic acids
- C07H21/02—Compounds containing two or more mononucleotide units having separate phosphate or polyphosphate groups linked by saccharide radicals of nucleoside groups, e.g. nucleic acids with ribosyl as saccharide radical
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- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07H—SUGARS; DERIVATIVES THEREOF; NUCLEOSIDES; NUCLEOTIDES; NUCLEIC ACIDS
- C07H21/00—Compounds containing two or more mononucleotide units having separate phosphate or polyphosphate groups linked by saccharide radicals of nucleoside groups, e.g. nucleic acids
- C07H21/04—Compounds containing two or more mononucleotide units having separate phosphate or polyphosphate groups linked by saccharide radicals of nucleoside groups, e.g. nucleic acids with deoxyribosyl as saccharide radical
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- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2319/00—Fusion polypeptide
- C07K2319/20—Fusion polypeptide containing a tag with affinity for a non-protein ligand
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- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2319/00—Fusion polypeptide
- C07K2319/35—Fusion polypeptide containing a fusion for enhanced stability/folding during expression, e.g. fusions with chaperones or thioredoxin
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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
- 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
-
- 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
- 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
- C12N15/66—General methods for inserting a gene into a vector to form a recombinant vector using cleavage and ligation; Use of non-functional linkers or adaptors, e.g. linkers containing the sequence for a restriction endonuclease
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- General Health & Medical Sciences (AREA)
- Medicinal Chemistry (AREA)
- Physics & Mathematics (AREA)
- Biophysics (AREA)
- Plant Pathology (AREA)
- Enzymes And Modification Thereof (AREA)
- Micro-Organisms Or Cultivation Processes Thereof (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
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| US28444409P | 2009-12-21 | 2009-12-21 | |
| US61/284,444 | 2009-12-21 | ||
| PCT/US2010/003225 WO2011084145A2 (en) | 2009-12-21 | 2010-12-21 | Recombinant butyrylcholinesterases and truncates thereof |
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| AU2010340358B2 true AU2010340358B2 (en) | 2014-07-24 |
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| AU (1) | AU2010340358B2 (https=) |
| CA (1) | CA2784861A1 (https=) |
| WO (1) | WO2011084145A2 (https=) |
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| Publication number | Priority date | Publication date | Assignee | Title |
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| JP2013526840A (ja) | 2009-12-21 | 2013-06-27 | ファーマシーネ，インコーポレイテッド | 組み換えブチリルコリンエステラーゼおよびその切断型 |
| US9688970B2 (en) | 2013-10-01 | 2017-06-27 | Kentucky Bioprocessing, Inc. | Plant-based recombinant butyrylcholinesterase production methods |
| LT3286209T (lt) * | 2015-04-24 | 2021-02-25 | Ferring Bv | Gonadotropino gamybos būdas |
| RU2021102893A (ru) * | 2015-11-05 | 2021-03-03 | Бамбу Терапьютикс, Инк. | Модифицированные гены атаксии фридрейха и векторы для генной терапии |
| CN108486114A (zh) * | 2018-04-18 | 2018-09-04 | 西南大学 | 实现两个基因等量表达的基因元件及表达载体 |
| EP3964265A1 (en) * | 2020-09-07 | 2022-03-09 | Fundacion Instituto De Investigacion Sanitaria Fundacion Jimenez Diaz | Mesenchymal stem cells co-expressing cxcr4 and il-10 and uses thereof |
Citations (2)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| WO2007040568A2 (en) * | 2004-12-01 | 2007-04-12 | Arizona Board Of Regents, Acting For And On Behalf Of Arizona State Univeristy | Production and use of human butyrylcholinesterase |
| US20080213281A1 (en) * | 2002-12-04 | 2008-09-04 | Applied Molecular Evolution, Inc. C/O Eli Lilly And Company Patent Division | Butyrylcholinesterase Variants that Alter the Activity of Chemotherapeutic Agents |
Family Cites Families (56)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US4179337A (en) | 1973-07-20 | 1979-12-18 | Davis Frank F | Non-immunogenic polypeptides |
| US6727405B1 (en) | 1986-04-09 | 2004-04-27 | Genzyme Corporation | Transgenic animals secreting desired proteins into milk |
| US5215909A (en) | 1986-06-18 | 1993-06-01 | Yeda Research & Development Co., Ltd. | Human cholinesterase genes |
| US5366894A (en) | 1986-06-30 | 1994-11-22 | Pharmaceutical Proteins Limited | Peptide production |
| EP0279582A3 (en) | 1987-02-17 | 1989-10-18 | Pharming B.V. | Dna sequences to target proteins to the mammary gland for efficient secretion |
| US5750172A (en) | 1987-06-23 | 1998-05-12 | Pharming B.V. | Transgenic non human mammal milk |
| US4873316A (en) | 1987-06-23 | 1989-10-10 | Biogen, Inc. | Isolation of exogenous recombinant proteins from the milk of transgenic mammals |
| FR2649991B2 (fr) | 1988-08-05 | 1994-03-04 | Rhone Poulenc Sante | Utilisation de derives stables du plasmide pkd1 pour l'expression et la secretion de proteines heterologues dans les levures du genre kluyveromyces |
| IL89703A (en) | 1989-03-21 | 2001-10-31 | Yissum Res Dev Co | Polynucleotide encoding human acetylcholinesterase, vectors comprising said polynucleotide, cells transformed by said vectors, enzyme produced by said transformed cell, and uses thereof |
| US5227301A (en) | 1989-11-03 | 1993-07-13 | The 501 Institution For The Advancement Of Learning (Mcgill University) | Immortalized bovine mannary epithelial cell line |
| US5633076A (en) | 1989-12-01 | 1997-05-27 | Pharming Bv | Method of producing a transgenic bovine or transgenic bovine embryo |
| US5831141A (en) | 1991-01-11 | 1998-11-03 | United States Of America As Represented By The Department Of Health And Human Services | Expression of a heterologous polypeptide in mammary tissue of transgenic non-human mammals using a long whey acidic protein promoter |
| IL101600A (en) | 1992-04-15 | 2000-02-29 | Yissum Res Dev Co | Synthetic partially phosphorothioated antisense oligodeoxynucleotides and pharmaceutical compositions containing them |
| US6110742A (en) | 1992-04-15 | 2000-08-29 | Yissum Research Development Company Of The Hebrew University Of Jerusalem | Synthetic antisense oligodeoxynucleotides targeted to AChE |
| DE69424687T2 (de) | 1993-03-09 | 2000-09-07 | Genzyme Corp., Cambridge | Verfahren zur isolierung von proteinen aus milch |
| US5610053A (en) | 1993-04-07 | 1997-03-11 | The United States Of America As Represented By The Department Of Health And Human Services | DNA sequence which acts as a chromatin insulator element to protect expressed genes from cis-acting regulatory sequences in mammalian cells |
| DE4326665C2 (de) | 1993-08-09 | 1995-07-13 | Biotest Pharma Gmbh | Verfahren zur Sterilfiltration von Milch |
| US6025183A (en) | 1994-02-28 | 2000-02-15 | Yissum Research Development Company Of The Hebrew University Of Jerusalem | Transgenic animal assay system for anti-cholinesterase substances |
| US5932780A (en) | 1994-02-28 | 1999-08-03 | Yissum Research Development Company Of Hebrew University Of Jerusalem | Transgenic non-human animal assay system for anti-cholinesterase substances |
| US6204431B1 (en) | 1994-03-09 | 2001-03-20 | Abbott Laboratories | Transgenic non-human mammals expressing heterologous glycosyltransferase DNA sequences produce oligosaccharides and glycoproteins in their milk |
| US5807671A (en) | 1995-01-09 | 1998-09-15 | Yissum Research Development Company Of Hebrew University Of Jerusalem | Method of screening for genetic predisposition to anticholinesterase therapy |
| US5780009A (en) | 1995-01-20 | 1998-07-14 | Nexia Biotechnologies, Inc. | Direct gene transfer into the ruminant mammary gland |
| US6001625A (en) | 1995-05-19 | 1999-12-14 | The United States Of America As Represented By The Secretary Of The Army | Site-directed mutagenesis of esterases |
| IL115873A0 (en) | 1995-11-03 | 1996-01-31 | Peri Dev Applic 1985 Ltd | Transgenic protein production |
| US6326139B1 (en) | 1996-01-11 | 2001-12-04 | Yissum Research Development Company Of Hebrew University Of Jerusalem | Method of screening for genetic predisposition to anticholinesterase therapy |
| US6268487B1 (en) | 1996-05-13 | 2001-07-31 | Genzyme Transgenics Corporation | Purification of biologically active peptides from milk |
| US20020184655A1 (en) | 1997-12-01 | 2002-12-05 | Henryk Lubon | Methods for the degradation and detoxification of organic material using urine produced by transgenic animals and related transgenic animals and proteins |
| US7157615B2 (en) | 1998-03-17 | 2007-01-02 | Nexia Biotechnologies, Inc. | Production of biofilaments in transgenic animals |
| DE69912444T3 (de) | 1998-08-25 | 2010-05-06 | University Of Washington, Seattle | Schnelle quantitative analyse von proteinen oder proteinfunktionen in komplexen gemischen |
| AU5755399A (en) | 1998-09-16 | 2000-04-03 | Nexia Biotechnologies, Inc. | Recombinant protein production in urine |
| US6580017B1 (en) | 1998-11-02 | 2003-06-17 | Genzyme Transgenics Corporation | Methods of reconstructed goat embryo transfer |
| WO2000029608A1 (en) | 1998-11-13 | 2000-05-25 | New York University | Transgenic animals as urinary bioreactors for the production of protein in the urine, recombinant dna construct for kidney-specific expression, and method of using same |
| EP1148779B1 (en) | 1999-01-06 | 2007-12-12 | Merrimack Pharmaceuticals, Inc. | Expression of secreted human alpha-fetoprotein in transgenic animals |
| US7297680B2 (en) | 1999-04-15 | 2007-11-20 | Crucell Holland B.V. | Compositions of erythropoietin isoforms comprising Lewis-X structures and high sialic acid content |
| IL146192A0 (en) | 1999-04-26 | 2002-07-25 | Us Army Med Res Mat Command | Differentially acting op detoxifying sponges |
| IL131707A0 (en) | 1999-05-31 | 2001-03-19 | Yissum Res Dev Co | Acetylcholinesterase-derived peptides and uses thereof |
| WO2001071014A2 (en) | 2000-03-17 | 2001-09-27 | Boyce Thompson Institute For Plant Research, Inc. | Expression of recombinant human acetylcholinesterase in transgenic plants |
| EP2206720A1 (en) | 2000-04-12 | 2010-07-14 | Human Genome Sciences, Inc. | Albumin fusion proteins |
| US6946134B1 (en) | 2000-04-12 | 2005-09-20 | Human Genome Sciences, Inc. | Albumin fusion proteins |
| US7070973B2 (en) | 2000-12-26 | 2006-07-04 | Board Of Regents Of The University Of Nebraska | Butyrylcholinesterase variants and methods of use |
| IL142875A (en) | 2001-04-30 | 2009-08-03 | Avigdor Shafferman | PEG-linked cholinesterases for the detoxification of circulating organophosphorus |
| JP2004535401A (ja) | 2001-05-21 | 2004-11-25 | ネクター セラピューティックス | 化学的に改変されたインスリンの肺投与 |
| CN1880457B (zh) * | 2001-10-11 | 2010-05-26 | 麦克公司 | Ad6重组核酸 |
| WO2003062374A2 (en) * | 2001-11-09 | 2003-07-31 | Entremed, Inc. | Synthetic genes for malarial proteins and methods of use |
| EP1458860A2 (en) | 2001-12-21 | 2004-09-22 | Nexia Biotechnologies, Inc. | Production of butyrylcholinesterases in transgenic mammals |
| WO2005035788A2 (en) | 2003-10-10 | 2005-04-21 | Yissum Research Development Company Of The Hebrew University Of Jerusalem | Method and kit for assessing anxiety or disposition thereto in a subject |
| EP2053409A1 (en) * | 2003-11-20 | 2009-04-29 | F. Hoffmann-La Roche Ag | Specific markers for metabolic syndrome |
| CA2551064A1 (en) | 2004-01-09 | 2005-07-21 | Yissum Research Development Company Of The Hebrew University Of Jerusale M | Compounds, pharmaceutical compositions and therapeutic methods of preventing and treating diseases and disorders associated with amyloid fibril formation |
| US20060194301A1 (en) | 2004-10-09 | 2006-08-31 | Doctor Bhupendra P | Large-scale production of human serum butyrylcholinesterase as a bioscavenger |
| WO2006063055A2 (en) | 2004-12-06 | 2006-06-15 | Bolder Biotechnology, Inc. | Enzyme conjugates for use as detoxifying agents |
| IL169377A (en) | 2005-06-23 | 2012-09-24 | Avigdor Shafferman | Uniformly conjugated serine hydrolases |
| DK2423315T3 (en) | 2006-06-29 | 2015-04-13 | Dsm Ip Assets Bv | A method for obtaining enhanced polypeptide expression |
| US20090208480A1 (en) | 2006-08-04 | 2009-08-20 | Yue Huang | Long half-life recombinant butyrylcholinesterase |
| ES2473623T3 (es) * | 2007-08-20 | 2014-07-07 | Glaxo Group Limited | Procedimiento de producción |
| US7846428B2 (en) * | 2007-10-05 | 2010-12-07 | Merial Limited | Articular cartilage gene therapy with recombinant vector encoding BMP-7 |
| JP2013526840A (ja) | 2009-12-21 | 2013-06-27 | ファーマシーネ，インコーポレイテッド | 組み換えブチリルコリンエステラーゼおよびその切断型 |
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Patent Citations (2)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US20080213281A1 (en) * | 2002-12-04 | 2008-09-04 | Applied Molecular Evolution, Inc. C/O Eli Lilly And Company Patent Division | Butyrylcholinesterase Variants that Alter the Activity of Chemotherapeutic Agents |
| WO2007040568A2 (en) * | 2004-12-01 | 2007-04-12 | Arizona Board Of Regents, Acting For And On Behalf Of Arizona State Univeristy | Production and use of human butyrylcholinesterase |
Non-Patent Citations (2)
| Title |
|---|
| Raymond et al, 2007, PloS ONE, vol 2, e152 * |
| Robinson et al, 2008, PLoS ONE, vol 3, e1801 * |
Also Published As
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| EP2516664A4 (en) | 2013-11-13 |
| US20140220658A1 (en) | 2014-08-07 |
| AU2010340358A1 (en) | 2012-07-19 |
| WO2011084145A2 (en) | 2011-07-14 |
| JP2013526840A (ja) | 2013-06-27 |
| US20120252094A1 (en) | 2012-10-04 |
| WO2011084145A3 (en) | 2013-05-30 |
| US8729245B2 (en) | 2014-05-20 |
| EP2516664A1 (en) | 2012-10-31 |
| EP2516664B1 (en) | 2015-07-22 |
| CA2784861A1 (en) | 2011-07-14 |
| US8952143B2 (en) | 2015-02-10 |
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