JP2015510770A - 組換えペプチドの産生方法 - Google Patents
組換えペプチドの産生方法 Download PDFInfo
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- JP2015510770A JP2015510770A JP2015500714A JP2015500714A JP2015510770A JP 2015510770 A JP2015510770 A JP 2015510770A JP 2015500714 A JP2015500714 A JP 2015500714A JP 2015500714 A JP2015500714 A JP 2015500714A JP 2015510770 A JP2015510770 A JP 2015510770A
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- Prior art keywords
- peptide
- vsdl
- fusion polypeptide
- cleavage site
- trypsin
- Prior art date
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- WHUUTDBJXJRKMK-VKHMYHEASA-N L-glutamic acid Chemical compound OC(=O)[C@@H](N)CCC(O)=O WHUUTDBJXJRKMK-VKHMYHEASA-N 0.000 description 1
- ZDXPYRJPNDTMRX-VKHMYHEASA-N L-glutamine Chemical compound OC(=O)[C@@H](N)CCC(N)=O ZDXPYRJPNDTMRX-VKHMYHEASA-N 0.000 description 1
- 101710175625 Maltose/maltodextrin-binding periplasmic protein Proteins 0.000 description 1
- 108010052285 Membrane Proteins Proteins 0.000 description 1
- 101710135898 Myc proto-oncogene protein Proteins 0.000 description 1
- 102100038895 Myc proto-oncogene protein Human genes 0.000 description 1
- 108700026244 Open Reading Frames Proteins 0.000 description 1
- 229920002845 Poly(methacrylic acid) Polymers 0.000 description 1
- 241000282405 Pongo abelii Species 0.000 description 1
- ONIBWKKTOPOVIA-UHFFFAOYSA-N Proline Natural products OC(=O)C1CCCN1 ONIBWKKTOPOVIA-UHFFFAOYSA-N 0.000 description 1
- 102000056251 Prolyl Oligopeptidases Human genes 0.000 description 1
- 108700015930 Prolyl Oligopeptidases Proteins 0.000 description 1
- 239000004365 Protease Substances 0.000 description 1
- 101800004937 Protein C Proteins 0.000 description 1
- 239000012564 Q sepharose fast flow resin Substances 0.000 description 1
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- 101800001700 Saposin-D Proteins 0.000 description 1
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- VYPSYNLAJGMNEJ-UHFFFAOYSA-N Silicium dioxide Chemical compound O=[Si]=O VYPSYNLAJGMNEJ-UHFFFAOYSA-N 0.000 description 1
- 108010088160 Staphylococcal Protein A Proteins 0.000 description 1
- 241000282898 Sus scrofa Species 0.000 description 1
- 108090001109 Thermolysin Proteins 0.000 description 1
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- 101710150448 Transcriptional regulator Myc Proteins 0.000 description 1
- 102400000757 Ubiquitin Human genes 0.000 description 1
- 108090000848 Ubiquitin Proteins 0.000 description 1
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- 230000002378 acidificating effect Effects 0.000 description 1
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- 201000011040 acute kidney failure Diseases 0.000 description 1
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- 238000013459 approach Methods 0.000 description 1
- 235000009582 asparagine Nutrition 0.000 description 1
- 229960001230 asparagine Drugs 0.000 description 1
- 230000001746 atrial effect Effects 0.000 description 1
- 108010005774 beta-Galactosidase Proteins 0.000 description 1
- 239000012620 biological material Substances 0.000 description 1
- 239000003729 cation exchange resin Substances 0.000 description 1
- 238000004113 cell culture Methods 0.000 description 1
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- ATDGTVJJHBUTRL-UHFFFAOYSA-N cyanogen bromide Chemical compound BrC#N ATDGTVJJHBUTRL-UHFFFAOYSA-N 0.000 description 1
- ZOOGRGPOEVQQDX-UHFFFAOYSA-N cyclic GMP Natural products O1C2COP(O)(=O)OC2C(O)C1N1C=NC2=C1NC(N)=NC2=O ZOOGRGPOEVQQDX-UHFFFAOYSA-N 0.000 description 1
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- 102000037865 fusion proteins Human genes 0.000 description 1
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- 125000003630 glycyl group Chemical group [H]N([H])C([H])([H])C(*)=O 0.000 description 1
- 208000019622 heart disease Diseases 0.000 description 1
- 238000004128 high performance liquid chromatography Methods 0.000 description 1
- 125000000487 histidyl group Chemical group [H]N([H])C(C(=O)O*)C([H])([H])C1=C([H])N([H])C([H])=N1 0.000 description 1
- 229910052588 hydroxylapatite Inorganic materials 0.000 description 1
- 238000001727 in vivo Methods 0.000 description 1
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- 238000005040 ion trap Methods 0.000 description 1
- 238000004895 liquid chromatography mass spectrometry Methods 0.000 description 1
- 210000004962 mammalian cell Anatomy 0.000 description 1
- 238000005374 membrane filtration Methods 0.000 description 1
- 238000002156 mixing Methods 0.000 description 1
- 235000015097 nutrients Nutrition 0.000 description 1
- 238000010979 pH adjustment Methods 0.000 description 1
- 239000008188 pellet Substances 0.000 description 1
- XYJRXVWERLGGKC-UHFFFAOYSA-D pentacalcium;hydroxide;triphosphate Chemical compound [OH-].[Ca+2].[Ca+2].[Ca+2].[Ca+2].[Ca+2].[O-]P([O-])([O-])=O.[O-]P([O-])([O-])=O.[O-]P([O-])([O-])=O XYJRXVWERLGGKC-UHFFFAOYSA-D 0.000 description 1
- 239000000546 pharmaceutical excipient Substances 0.000 description 1
- 230000035479 physiological effects, processes and functions Effects 0.000 description 1
- 150000003109 potassium Chemical class 0.000 description 1
- 238000001556 precipitation Methods 0.000 description 1
- 108010064037 prorennin Proteins 0.000 description 1
- 229960000856 protein c Drugs 0.000 description 1
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Classifications
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/435—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
- C07K14/575—Hormones
- C07K14/58—Atrial natriuretic factor complex; Atriopeptin; Atrial natriuretic peptide [ANP]; Cardionatrin; Cardiodilatin
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/435—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
- C07K14/575—Hormones
-
- 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
- C12N15/11—DNA or RNA fragments; Modified forms thereof; Non-coding nucleic acids having a biological activity
- C12N15/62—DNA sequences coding for fusion proteins
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12P—FERMENTATION OR ENZYME-USING PROCESSES TO SYNTHESISE A DESIRED CHEMICAL COMPOUND OR COMPOSITION OR TO SEPARATE OPTICAL ISOMERS FROM A RACEMIC MIXTURE
- C12P21/00—Preparation of peptides or proteins
- C12P21/06—Preparation of peptides or proteins produced by the hydrolysis of a peptide bond, e.g. hydrolysate products
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2319/00—Fusion polypeptide
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2319/00—Fusion polypeptide
- C07K2319/50—Fusion polypeptide containing protease site
Landscapes
- Health & Medical Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Chemical & Material Sciences (AREA)
- Genetics & Genomics (AREA)
- Organic Chemistry (AREA)
- Engineering & Computer Science (AREA)
- Zoology (AREA)
- Molecular Biology (AREA)
- Wood Science & Technology (AREA)
- General Health & Medical Sciences (AREA)
- Biochemistry (AREA)
- Biomedical Technology (AREA)
- Biophysics (AREA)
- General Engineering & Computer Science (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Biotechnology (AREA)
- Gastroenterology & Hepatology (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Medicinal Chemistry (AREA)
- Endocrinology (AREA)
- Toxicology (AREA)
- Microbiology (AREA)
- Physics & Mathematics (AREA)
- Plant Pathology (AREA)
- Chemical Kinetics & Catalysis (AREA)
- General Chemical & Material Sciences (AREA)
- Cardiology (AREA)
- Peptides Or Proteins (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
- Micro-Organisms Or Cultivation Processes Thereof (AREA)
- Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
Applications Claiming Priority (3)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| US201261612817P | 2012-03-19 | 2012-03-19 | |
| US61/612,817 | 2012-03-19 | ||
| PCT/AU2013/000273 WO2013138850A1 (en) | 2012-03-19 | 2013-03-19 | Method of producing a recombinant peptide |
Publications (2)
| Publication Number | Publication Date |
|---|---|
| JP2015510770A true JP2015510770A (ja) | 2015-04-13 |
| JP2015510770A5 JP2015510770A5 (enExample) | 2016-05-19 |
Family
ID=49221695
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| JP2015500714A Pending JP2015510770A (ja) | 2012-03-19 | 2013-03-19 | 組換えペプチドの産生方法 |
Country Status (8)
| Country | Link |
|---|---|
| US (1) | US20150315259A1 (enExample) |
| EP (1) | EP2839010B1 (enExample) |
| JP (1) | JP2015510770A (enExample) |
| KR (1) | KR20140148420A (enExample) |
| CN (2) | CN107266554A (enExample) |
| AU (2) | AU2013234860B2 (enExample) |
| SG (1) | SG11201405721VA (enExample) |
| WO (1) | WO2013138850A1 (enExample) |
Families Citing this family (3)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US8947194B2 (en) | 2009-05-26 | 2015-02-03 | Solaredge Technologies Ltd. | Theft detection and prevention in a power generation system |
| EP3773669A4 (en) * | 2018-03-29 | 2022-04-27 | Contrafect Corporation | ANTIMICROBIAL BACTERIOPHAGE-DERIVED POLYPEPTIDES AND THEIR USE AGAINST GRAM-NEGATIVE BACTERIA |
| CN113121637B (zh) * | 2020-01-15 | 2022-06-14 | 鲁南制药集团股份有限公司 | 一种重组蛋白的分离纯化方法 |
Citations (5)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| JP2001512745A (ja) * | 1997-08-07 | 2001-08-28 | クリエイティヴ・ペプティドス・スウェーデン・アクチエボラーグ | インスリンc−ペプチドの組換え発現 |
| JP2004519417A (ja) * | 2000-06-30 | 2004-07-02 | ベクトン・ディキンソン・アンド・カンパニー | 培地用ペプチド |
| JP2006508639A (ja) * | 2002-05-24 | 2006-03-16 | リストレイジェン・インコーポレイテッド | ポリペプチドの高収率生産のための方法およびdna構築物 |
| WO2009040031A2 (en) * | 2007-09-11 | 2009-04-02 | Mondobiotech Laboratories Ag | Use of a peptide as a therapeutic agent |
| US20110008827A1 (en) * | 2008-06-18 | 2011-01-13 | Isfahan University Of Technology | Method to produce recombinant MBP8298 and other polypeptides by nucleotide structure optimization |
Family Cites Families (11)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US5691310A (en) | 1987-09-29 | 1997-11-25 | Vesely; David L. | Methods of treatment using proANF peptides |
| ES2263278T3 (es) * | 1998-07-10 | 2006-12-01 | Scios Inc. | Metodo para producir un peptido con un pl por encima de 8 o por debajo de 5. |
| WO2000017336A1 (en) * | 1998-09-19 | 2000-03-30 | Sang Jun Lee | Dna cassette encoding a multimer of a biologically active peptide and a cleavable linker attached thereto and process for preparing the biologically active peptide |
| CN1363654A (zh) * | 2001-07-19 | 2002-08-14 | 上海华谊生物技术有限公司 | 生产促胰岛素分泌肽glp-1(7-36)的基因工程菌以及生产glp-1(7-36)的方法 |
| DE60331584D1 (de) * | 2002-11-26 | 2010-04-15 | Biocon Ltd | Modifizierte natriuretic verbindungen, konjugate und ihre verwendungen |
| WO2005094420A2 (en) * | 2004-02-17 | 2005-10-13 | University Of South Florida | Materials and methods for treatment of inflammatory and cell proliferation disorders |
| EP1736480B9 (en) * | 2005-06-02 | 2009-03-04 | Polyquant GmbH | Artificial protein, method for absolute quantification of proteins and uses thereof |
| RU2451750C2 (ru) * | 2007-09-24 | 2012-05-27 | Общество С Ограниченной Ответственностью "Герофарм" | Способ получения рекомбинантного с-пептида проинсулина человека |
| JP2013505013A (ja) * | 2009-09-18 | 2013-02-14 | セレクシス エス.エー. | 強化導入遺伝子発現およびプロセッシングの産物および方法 |
| WO2012019237A1 (en) * | 2010-08-12 | 2012-02-16 | Madeleine Pharmaceuticals Pty Ltd | Therapeutic method for treating congestive heart failure |
| WO2012115772A2 (en) * | 2011-02-25 | 2012-08-30 | Medtronic, Inc. | Therapy for kidney disease and/or heart failure |
-
2013
- 2013-03-19 JP JP2015500714A patent/JP2015510770A/ja active Pending
- 2013-03-19 US US14/385,402 patent/US20150315259A1/en not_active Abandoned
- 2013-03-19 CN CN201710409638.4A patent/CN107266554A/zh active Pending
- 2013-03-19 EP EP13765199.8A patent/EP2839010B1/en active Active
- 2013-03-19 KR KR1020147029054A patent/KR20140148420A/ko not_active Withdrawn
- 2013-03-19 WO PCT/AU2013/000273 patent/WO2013138850A1/en not_active Ceased
- 2013-03-19 AU AU2013234860A patent/AU2013234860B2/en not_active Ceased
- 2013-03-19 CN CN201380025049.6A patent/CN104364378A/zh active Pending
- 2013-03-19 SG SG11201405721VA patent/SG11201405721VA/en unknown
-
2016
- 2016-02-29 AU AU2016100212A patent/AU2016100212A4/en not_active Ceased
Patent Citations (5)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| JP2001512745A (ja) * | 1997-08-07 | 2001-08-28 | クリエイティヴ・ペプティドス・スウェーデン・アクチエボラーグ | インスリンc−ペプチドの組換え発現 |
| JP2004519417A (ja) * | 2000-06-30 | 2004-07-02 | ベクトン・ディキンソン・アンド・カンパニー | 培地用ペプチド |
| JP2006508639A (ja) * | 2002-05-24 | 2006-03-16 | リストレイジェン・インコーポレイテッド | ポリペプチドの高収率生産のための方法およびdna構築物 |
| WO2009040031A2 (en) * | 2007-09-11 | 2009-04-02 | Mondobiotech Laboratories Ag | Use of a peptide as a therapeutic agent |
| US20110008827A1 (en) * | 2008-06-18 | 2011-01-13 | Isfahan University Of Technology | Method to produce recombinant MBP8298 and other polypeptides by nucleotide structure optimization |
Non-Patent Citations (1)
| Title |
|---|
| SANG JUN LEE, ET AL, MOLECULES AND CELLS, vol. 10, no. 2, JPN6017013630, 2000, pages 236 - 240 * |
Also Published As
| Publication number | Publication date |
|---|---|
| CN104364378A (zh) | 2015-02-18 |
| EP2839010B1 (en) | 2018-04-25 |
| AU2016100212A4 (en) | 2016-04-14 |
| CN107266554A (zh) | 2017-10-20 |
| EP2839010A4 (en) | 2015-12-09 |
| KR20140148420A (ko) | 2014-12-31 |
| EP2839010A1 (en) | 2015-02-25 |
| US20150315259A1 (en) | 2015-11-05 |
| WO2013138850A1 (en) | 2013-09-26 |
| AU2013234860A1 (en) | 2014-10-16 |
| SG11201405721VA (en) | 2014-10-30 |
| AU2013234860B2 (en) | 2016-01-21 |
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