FI86886C - Nya expressionsplasmider och deras anvaendning i foerfarandet foer expressering av prokymosin koderande gen i e. coli - Google Patents
Nya expressionsplasmider och deras anvaendning i foerfarandet foer expressering av prokymosin koderande gen i e. coli Download PDFInfo
- Publication number
- FI86886C FI86886C FI840918A FI840918A FI86886C FI 86886 C FI86886 C FI 86886C FI 840918 A FI840918 A FI 840918A FI 840918 A FI840918 A FI 840918A FI 86886 C FI86886 C FI 86886C
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- FI
- Finland
- Prior art keywords
- plasmid
- dna
- ecori
- map shown
- prochymosin
- Prior art date
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Classifications
-
- 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)
- C12N9/64—Proteinases, e.g. Endopeptidases (3.4.21-3.4.25) derived from animal tissue
- C12N9/6421—Proteinases, e.g. Endopeptidases (3.4.21-3.4.25) derived from animal tissue from mammals
- C12N9/6478—Aspartic endopeptidases (3.4.23)
- C12N9/6481—Pepsins (3.4.23.1; 3.4.23.2; 3.4.23.3)
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K1/00—General methods for the preparation of peptides, i.e. processes for the organic chemical preparation of peptides or proteins of any length
- C07K1/107—General methods for the preparation of peptides, i.e. processes for the organic chemical preparation of peptides or proteins of any length by chemical modification of precursor peptides
- C07K1/113—General methods for the preparation of peptides, i.e. processes for the organic chemical preparation of peptides or proteins of any length by chemical modification of precursor peptides without change of the primary structure
- C07K1/1136—General methods for the preparation of peptides, i.e. processes for the organic chemical preparation of peptides or proteins of any length by chemical modification of precursor peptides without change of the primary structure by reversible modification of the secondary, tertiary or quarternary structure, e.g. using denaturating or stabilising agents
-
- 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
- C12N15/70—Vectors or expression systems specially adapted for E. coli
- C12N15/71—Expression systems using regulatory sequences derived from the trp-operon
-
- 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)
- C12N9/64—Proteinases, e.g. Endopeptidases (3.4.21-3.4.25) derived from animal tissue
- C12N9/6421—Proteinases, e.g. Endopeptidases (3.4.21-3.4.25) derived from animal tissue from mammals
- C12N9/6478—Aspartic endopeptidases (3.4.23)
- C12N9/6483—Chymosin (3.4.23.4), i.e. rennin
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12Y—ENZYMES
- C12Y304/00—Hydrolases acting on peptide bonds, i.e. peptidases (3.4)
- C12Y304/23—Aspartic endopeptidases (3.4.23)
- C12Y304/23004—Chymosin (3.4.23.4), i.e. rennin
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2319/00—Fusion polypeptide
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- Chemical & Material Sciences (AREA)
- Health & Medical Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Engineering & Computer Science (AREA)
- Organic Chemistry (AREA)
- Genetics & Genomics (AREA)
- Wood Science & Technology (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Zoology (AREA)
- Biomedical Technology (AREA)
- General Engineering & Computer Science (AREA)
- Biochemistry (AREA)
- General Health & Medical Sciences (AREA)
- Biotechnology (AREA)
- Molecular Biology (AREA)
- Medicinal Chemistry (AREA)
- Microbiology (AREA)
- Biophysics (AREA)
- Plant Pathology (AREA)
- Physics & Mathematics (AREA)
- Crystallography & Structural Chemistry (AREA)
- Chemical Kinetics & Catalysis (AREA)
- General Chemical & Material Sciences (AREA)
- Analytical Chemistry (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Micro-Organisms Or Cultivation Processes Thereof (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
- Enzymes And Modification Thereof (AREA)
- Saccharide Compounds (AREA)
Applications Claiming Priority (2)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| JP58038439A JPS59166086A (ja) | 1983-03-09 | 1983-03-09 | 新規な発現型プラスミドとそれらを用いて仔牛プロキモシン遺伝子を大腸菌内で発現させる方法 |
| JP3843983 | 1983-03-09 |
Publications (4)
| Publication Number | Publication Date |
|---|---|
| FI840918A0 FI840918A0 (fi) | 1984-03-07 |
| FI840918L FI840918L (fi) | 1984-09-10 |
| FI86886B FI86886B (fi) | 1992-07-15 |
| FI86886C true FI86886C (fi) | 1992-10-26 |
Family
ID=12525334
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| FI840918A FI86886C (fi) | 1983-03-09 | 1984-03-07 | Nya expressionsplasmider och deras anvaendning i foerfarandet foer expressering av prokymosin koderande gen i e. coli |
Country Status (9)
| Country | Link |
|---|---|
| EP (1) | EP0121775A1 (https=) |
| JP (1) | JPS59166086A (https=) |
| AR (1) | AR241795A1 (https=) |
| AU (1) | AU572827B2 (https=) |
| BR (1) | BR8401049A (https=) |
| DK (1) | DK136184A (https=) |
| FI (1) | FI86886C (https=) |
| IE (1) | IE57264B1 (https=) |
| NZ (1) | NZ207414A (https=) |
Families Citing this family (72)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| EP0123928A3 (en) * | 1983-03-31 | 1986-02-05 | Codon Genetic Engineering Laboratories | Recombinant dna coding for a polypeptide displaying milk clotting activity |
| US4721673A (en) * | 1983-09-01 | 1988-01-26 | Genex Corporation | Recovery and activation process for microbially produced calf prochymosin |
| JPS60188093A (ja) * | 1984-03-09 | 1985-09-25 | Teruhiko Beppu | 枯草菌に於ける形質発現プラスミド |
| JPS60188077A (ja) * | 1984-03-09 | 1985-09-25 | Teruhiko Beppu | 仔牛プロキモシンｃＤΝＡの全配列を有する新規な発現プラスミド |
| US5082775A (en) * | 1984-05-11 | 1992-01-21 | Berlex Laboratories, Inc. | Efficient process for isolating insoluble heterologous protein using non-ionic detergents |
| US4705848A (en) * | 1986-06-02 | 1987-11-10 | International Minerals & Chemical Corp. | Isolation of bioactive, monomeric growth hormone |
| GB2200118A (en) * | 1987-01-23 | 1988-07-27 | Allelix Inc | Synthetic chymosin-and prochymosin-encoding DNA segments |
| JP4236698B2 (ja) | 1990-11-26 | 2009-03-11 | ジェネティックス インスティチュート，リミテッド ライアビリティ カンパニー | 宿主細胞でのｐａｃｅの発現およびその使用法 |
| US5629167A (en) | 1994-04-19 | 1997-05-13 | Biocine S.P.A. | Detection of antibodies against Chlamydia trachomatis pgp3 antigen in patient sera by enzyme-linked immunosorbent assay |
| CN1263854C (zh) | 1997-11-06 | 2006-07-12 | 启龙股份公司 | 奈瑟球菌抗原 |
| AU1979599A (en) | 1998-01-14 | 1999-08-02 | Chiron S.P.A. | (neisseria meningitidis) antigens |
| GB9808932D0 (en) | 1998-04-27 | 1998-06-24 | Chiron Spa | Polyepitope carrier protein |
| EP2261352A3 (en) | 1998-05-01 | 2012-01-04 | Novartis Vaccines and Diagnostics, Inc. | Neisseria meningitidis antigens and compositions |
| JP2003518363A (ja) | 1999-04-30 | 2003-06-10 | カイロン エセ．ピー．アー． | 保存されたナイセリア抗原 |
| GB9911683D0 (en) | 1999-05-19 | 1999-07-21 | Chiron Spa | Antigenic peptides |
| GB9916529D0 (en) | 1999-07-14 | 1999-09-15 | Chiron Spa | Antigenic peptides |
| RU2281956C2 (ru) | 1999-10-29 | 2006-08-20 | Чирон С.Р.Л. | Антигенные пептиды neisseria |
| PT2289545T (pt) | 2000-01-17 | 2016-09-06 | Glaxosmithkline Biologicals Sa | Vacina de omv suplementada contra meningococos |
| DK1328543T3 (da) | 2000-10-27 | 2009-11-23 | Novartis Vaccines & Diagnostic | Nukleinsyrer og proteiner fra streptococcus-gruppe A & B |
| EP1334182B2 (en) | 2000-11-06 | 2021-03-24 | Chr. Hansen A/S | Method of producing non-bovine chymosin and use hereof |
| GB0107658D0 (en) | 2001-03-27 | 2001-05-16 | Chiron Spa | Streptococcus pneumoniae |
| GB0107661D0 (en) | 2001-03-27 | 2001-05-16 | Chiron Spa | Staphylococcus aureus |
| BR0211494A (pt) | 2001-07-27 | 2004-08-17 | Chiron Srl | Adesinas de meningococo nada, app e orf 40 |
| CN100515494C (zh) | 2001-12-12 | 2009-07-22 | 启龙有限公司 | 抗沙眼衣原体的免疫 |
| AU2003239865A1 (en) | 2002-05-24 | 2003-12-12 | Restoragen Inc. | Method for universal enzymatic production of bioactive peptides |
| EP1572720A4 (en) | 2002-05-24 | 2008-12-24 | Nps Allelix Corp | PROCESS FOR THE ENZYMATIC PRODUCTION OF GLP-2 (1-34) AND GLP-2 (1-33) PEPTIDES |
| EP1562982B1 (en) | 2002-11-15 | 2010-05-05 | Novartis Vaccines and Diagnostics S.r.l. | Unexpected surface proteins in neisseria meningitidis |
| GB0227346D0 (en) | 2002-11-22 | 2002-12-31 | Chiron Spa | 741 |
| GB0308198D0 (en) | 2003-04-09 | 2003-05-14 | Chiron Srl | ADP-ribosylating bacterial toxin |
| AU2004235346A1 (en) | 2003-04-25 | 2004-11-11 | North Carolina State University | Lactobacillus acidophilus nucleic acid sequences encoding cell surface protein homologues and uses therefore |
| DE602004032144D1 (de) | 2003-06-23 | 2011-05-19 | Univ North Carolina State | Für fructooligosaccharid-nutzende verbindungen codierende nukleinsäuren aus lactobacillus acidophilus und verwendungen davon |
| WO2005067368A2 (en) | 2003-11-21 | 2005-07-28 | Nps Allelix Corp. | Production of glucagon like peptide 2 and analogs |
| EP2327724A3 (en) | 2004-02-02 | 2011-07-27 | Ambrx, Inc. | Modified human growth hormone polypeptides and their uses |
| US7459289B2 (en) | 2004-03-08 | 2008-12-02 | North Carolina State University | Lactobacillus acidophilus nucleic acid sequences encoding carbohydrate utilization-related proteins and uses therefor |
| KR101699142B1 (ko) | 2004-06-18 | 2017-01-23 | 암브룩스, 인코포레이티드 | 신규 항원-결합 폴리펩티드 및 이의 용도 |
| JP2008507280A (ja) | 2004-07-21 | 2008-03-13 | アンブレツクス・インコーポレイテツド | 非天然コードアミノ酸を用いた生合成ポリペプチド |
| EP1828224B1 (en) | 2004-12-22 | 2016-04-06 | Ambrx, Inc. | Compositions containing, methods involving, and uses of non-natural amino acids and polypeptides |
| JP2008525473A (ja) | 2004-12-22 | 2008-07-17 | アンブレツクス・インコーポレイテツド | 修飾されたヒト成長ホルモン |
| AU2006236629B2 (en) | 2005-04-15 | 2012-04-19 | North Carolina State University | Methods and compositions to modulate adhesion and stress tolerance in bacteria |
| EP1951890A4 (en) | 2005-11-16 | 2009-06-24 | Ambrx Inc | PROCESSES AND COMPOSITIONS WITH NON-NATURAL AMINO ACIDS |
| GB0524066D0 (en) | 2005-11-25 | 2006-01-04 | Chiron Srl | 741 ii |
| DK2054431T3 (da) | 2006-06-09 | 2012-01-02 | Novartis Ag | Konformere af bakterielle adhæsiner |
| CN106008699A (zh) | 2006-09-08 | 2016-10-12 | Ambrx公司 | 经修饰的人类血浆多肽或Fc骨架和其用途 |
| CA2682147C (en) | 2007-03-30 | 2017-08-08 | Ambrx, Inc. | Modified fgf-21 polypeptides and their uses |
| MX2010005317A (es) | 2007-11-20 | 2010-06-02 | Ambrx Inc | Polipeptidos de insulina modificados y sus usos. |
| NZ586947A (en) | 2008-02-08 | 2012-11-30 | Ambrx Inc | Modified leptin polypeptides and their uses |
| CN102356089B (zh) | 2008-02-21 | 2014-02-19 | 诺华股份有限公司 | 脑膜炎球菌fHBP多肽 |
| PT2318029T (pt) | 2008-07-23 | 2018-01-10 | Ambrx Inc | Polipéptidos de g-csf bovino modificados e suas utilizações |
| PE20110480A1 (es) | 2008-09-26 | 2011-07-01 | Ambrx Inc | Microorganismos y vacunas dependientes de replicacion de aminoacidos no naturales |
| MX2011003272A (es) | 2008-09-26 | 2011-04-28 | Ambrx Inc | Polipeptidos de eritropoyetina animal modificados y sus usos. |
| US20110076300A1 (en) | 2009-08-27 | 2011-03-31 | Mariagrazia Pizza | Hybrid Polypeptides Including Meningococcal fHBP Sequences |
| CA2779816A1 (en) | 2009-10-27 | 2011-05-05 | Novartis Ag | Modified meningococcal fhbp polypeptides |
| JP2013515081A (ja) | 2009-12-21 | 2013-05-02 | アンブルックス，インコーポレイテッド | 修飾されているブタのソマトトロピンポリペプチドおよびそれらの使用 |
| NZ600361A (en) | 2009-12-21 | 2014-06-27 | Ambrx Inc | Modified bovine somatotropin polypeptides and their uses |
| EP2571894A1 (en) | 2010-05-19 | 2013-03-27 | North Carolina State University | Compositions and methods for the delivery of therapeutic peptides |
| MA34521B1 (fr) | 2010-08-17 | 2013-09-02 | Ambrx Inc | Polypeptides de relaxine modifiés et leurs utilisations |
| US9567386B2 (en) | 2010-08-17 | 2017-02-14 | Ambrx, Inc. | Therapeutic uses of modified relaxin polypeptides |
| TWI480288B (zh) | 2010-09-23 | 2015-04-11 | Lilly Co Eli | 牛顆粒細胞群落刺激因子及其變體之調配物 |
| RU2473683C1 (ru) * | 2011-12-15 | 2013-01-27 | Общество С Ограниченной Ответственностью "Фармапарк" | СПОСОБ ПРОМЫШЛЕННОГО КУЛЬТИВИРОВАНИЯ ШТАММОВ E.coli, ПОЛУЧЕННЫХ НА ОСНОВЕ ШТАММА BL21(DE3), НЕСУЩЕГО ГЕН T7 RNA ПОЛИМЕРАЗЫ ПОД КОНТРОЛЕМ lacUV5 ПРОМОТОРА, С ПОВЫШЕННЫМ СИНТЕЗОМ БИОМАССЫ И ВЫХОДОМ ЦЕЛЕВОГО БЕЛКА В ТЕЛЬЦАХ ВКЛЮЧЕНИЯ |
| EP3060656A1 (en) | 2013-10-24 | 2016-08-31 | Yeda Research and Development Co., Ltd. | Polynucleotides encoding brex system polypeptides and methods of using same |
| SMT202100388T1 (it) | 2014-10-24 | 2021-09-14 | Bristol Myers Squibb Co | Polipeptidi fgf-21 modificati e loro usi |
| US10590426B2 (en) | 2016-08-22 | 2020-03-17 | Board Of Trustees Of Michigan State University | Genetic control of cell size |
| IL250479A0 (en) | 2017-02-06 | 2017-03-30 | Sorek Rotem | Genetically engineered cells expressing a disarm system that confers resistance to phages and methods for their production |
| CN110637027B (zh) | 2017-02-08 | 2024-08-30 | 百时美施贵宝公司 | 包含药代动力学增强子的修饰的松弛素多肽及其用途 |
| CN107881162A (zh) * | 2017-12-25 | 2018-04-06 | 中诺生物科技发展江苏有限公司 | 一种工业化生产凝乳酶的方法 |
| IL258467A (en) | 2018-03-29 | 2018-07-04 | Ilana Kolodkin Gal | Methods of disrupting a biofilm and/or preventing formation of same |
| HRP20240016T1 (hr) | 2018-09-11 | 2024-03-29 | Ambrx, Inc. | Konjugati polipeptida interleukina-2 i njihove uporabe |
| EP3946611A2 (en) | 2019-03-31 | 2022-02-09 | Yeda Research and Development Co. Ltd | Anti-viral and anti-tumoral compounds |
| WO2021183832A1 (en) | 2020-03-11 | 2021-09-16 | Ambrx, Inc. | Interleukin-2 polypeptide conjugates and methods of use thereof |
| WO2022038539A2 (en) | 2020-08-18 | 2022-02-24 | Yeda Research And Development Co. Ltd. | Anti-viral and anti-tumoral compounds |
| IL288680A (en) | 2021-12-05 | 2023-07-01 | Yeda Res & Dev | Genetically modified phages and their use |
| WO2025215636A1 (en) | 2024-04-08 | 2025-10-16 | Yeda Research And Development Co. Ltd. | Anti-defense system polypeptides and uses thereof |
Family Cites Families (7)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US4666847A (en) * | 1981-01-16 | 1987-05-19 | Collaborative Research, Inc. | Recombinant DNA means and method |
| JPS589687A (ja) * | 1981-06-17 | 1983-01-20 | セルテク リミテッド | ポリペプチドの生産方法 |
| IE53517B1 (en) * | 1981-06-17 | 1988-12-07 | Celltech Ltd | Process for the production of a polypeptide |
| JPS5832896A (ja) * | 1981-08-24 | 1983-02-25 | Teruhiko Beppu | 複合プラスミド及びそれを含有する微生物 |
| BR8205954A (pt) * | 1981-10-14 | 1983-09-13 | Unilever Nv | Sequencia de dna,plasmidio recombinante,cultura bacteriana e microorganismos |
| ZA834095B (en) * | 1982-07-01 | 1984-02-29 | Genex Corp | Bovine calf chymosin |
| IE56372B1 (en) * | 1982-12-22 | 1991-07-03 | Genentech Inc | Microbially produced rennet methods for its production and plasmids used for its production |
-
1983
- 1983-03-09 JP JP58038439A patent/JPS59166086A/ja active Granted
-
1984
- 1984-02-29 DK DK136184A patent/DK136184A/da not_active Application Discontinuation
- 1984-03-07 EP EP84102451A patent/EP0121775A1/en not_active Withdrawn
- 1984-03-07 FI FI840918A patent/FI86886C/fi not_active IP Right Cessation
- 1984-03-07 AU AU25357/84A patent/AU572827B2/en not_active Ceased
- 1984-03-07 NZ NZ207414A patent/NZ207414A/en unknown
- 1984-03-08 IE IE559/84A patent/IE57264B1/en not_active IP Right Cessation
- 1984-03-08 BR BR8401049A patent/BR8401049A/pt unknown
- 1984-03-09 AR AR84295974A patent/AR241795A1/es active
Also Published As
| Publication number | Publication date |
|---|---|
| AU2535784A (en) | 1984-09-13 |
| DK136184A (da) | 1984-09-10 |
| EP0121775A1 (en) | 1984-10-17 |
| BR8401049A (pt) | 1984-10-16 |
| IE840559L (en) | 1984-09-09 |
| JPS59166086A (ja) | 1984-09-19 |
| AR241795A1 (es) | 1992-12-30 |
| IE57264B1 (en) | 1992-07-01 |
| NZ207414A (en) | 1988-02-29 |
| JPS6240999B2 (https=) | 1987-09-01 |
| FI86886B (fi) | 1992-07-15 |
| DK136184D0 (da) | 1984-02-29 |
| FI840918L (fi) | 1984-09-10 |
| AU572827B2 (en) | 1988-05-19 |
| FI840918A0 (fi) | 1984-03-07 |
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Legal Events
| Date | Code | Title | Description |
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| MM | Patent lapsed |
Owner name: BEPPU, TERUHIKO |